Course Information

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (seminar tutor)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Timetable

Mon 19. 2. to Sun 26. 5. Fri 9:00–9:50 Kontaktujte učitele, Fri 10:00–10:50 Kontaktujte učitele

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (seminar tutor)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Taught in person.

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Taught in person.

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (seminar tutor)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Timetable

Fri 9:00–9:50 Kontaktujte učitele, Fri 10:00–10:50 Kontaktujte učitele

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Taught in person.

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Timetable

Fri 9:00–9:50 Kontaktujte učitele, Fri 10:00–10:50 Kontaktujte učitele

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Taught in person.

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Timetable

Mon 1. 3. to Fri 14. 5. Fri 9:00–9:50 C04/118, Fri 10:00–10:50 C04/211

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Taught in person.

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Timetable

Fri 9:00–9:50 C04/57, Fri 10:00–10:50 C04/57

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Learning outcomes

At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
Mgr. Pavel Kadeřávek, Ph.D. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Practical NMR Spectroscopy of Biomolecules

Extent and Intensity

1/0/1. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
doc. Mgr. Karel Kubíček, PhD. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have basic knowledge of NMR theory, previous passing the course C5320 is an advantage but not absolutely necessary.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on experience with using NMR spectrometers with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to use independently the sophisticated NMR instrumentation for routine measurements of spectra of proteins and nucleic acids, as well as most other common samples.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. 1D proton spectroscopy and water suppression techniques 5. 1D NMR spectroscopy of nuclei other than H-1 6. Homonuclear 2D experiments 7. Heteronuclear experiments for natural abundance and isotopically labeled samples 8. Data processing, apodization functions, linear prediction, non-uniform sampling 9. Analysis of protein NMR spectra 10. Analysis of NMR spectra of nucleic acids

Literature

recommended literature
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Teaching methods

Lectures plus laboratory practice

Assessment methods

Written test of NMR theory plus test of practical operation of the NMR spectrometer.

Language of instruction

English

Follow-Up Courses

• C6770 NMR Spectroscopy of Biomolecules

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://www.ncbr.muni.cz/~fiala/

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

At the end of the course students should have hands-on knowledge of sophisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

At the end of the course students should have hands-on knowledge of sophisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sophisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

Study Materials
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup 3. Spectrometer calibrations 4. Building blocks of pulse sequences 5. Programming of pulse sequences 6. Water suppression techniques 7. Homonuclear 2D experiments 8. Heteronuclear double and triple resonance experiments 9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN) 10. Data processing 11. Analysis of protein NMR spectra 12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Assessment methods (in Czech)

Presence in practical sessions at the spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup 3. Spectrometer calibrations 4. Building blocks of pulse sequences 5. Programming of pulse sequences 6. Water suppression techniques 7. Homonuclear 2D experiments 8. Heteronuclear double and triple resonance experiments 9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN) 10. Data processing 11. Analysis of protein NMR spectra 12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Assessment methods (in Czech)

Presence in practical sessions at the spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup 3. Spectrometer calibrations 4. Building blocks of pulse sequences 5. Programming of pulse sequences 6. Water suppression techniques 7. Homonuclear 2D experiments 8. Heteronuclear double and triple resonance experiments 9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN) 10. Data processing 11. Analysis of protein NMR spectra 12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Assessment methods (in Czech)

Presence in practical sessions at the spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Syllabus

• 1. NMR sample, preparation and handling 2. Spectrometer setup and calibrations 3. Pulse sequence programming 4. 2D and 3D heteronuclear experiments for proteins and nucleic acids 5. Data processing and analysis

Assessment methods (in Czech)

Presence in practical sessions at the spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course is taught annually.
The course is taught: in blocks.

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Assessment methods (in Czech)

Presence in practical sessions at spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course is taught annually.
The course is taught: in blocks.

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Assessment methods (in Czech)

Presence in practical sessions at spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course is taught annually.
The course is taught: in blocks.

C7995 Advanced Methods of Biomolecular NMR

The information about the term Autumn 2011 - acreditation is not made public

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup
  3. Spectrometer calibrations
  4. Building blocks of pulse sequences
  5. Programming of pulse sequences
  6. Water suppression techniques
  7. Homonuclear 2D experiments
  8. Heteronuclear double and triple resonance experiments
  9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN)
  10. Data processing
  11. Analysis of protein NMR spectra
  12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
• CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
• BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
• CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info

Teaching methods

Lectures, laboratory practice, work on a project

Assessment methods

Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

C7995 Advanced Methods of Biomolecular NMR

Extent and Intensity

2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).

Teacher(s)

doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)

Guaranteed by

doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.

Prerequisites

Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.

Course Enrolment Limitations

The course is also offered to the students of the fields other than those the course is directly associated with.

fields of study / plans the course is directly associated with

there are 6 fields of study the course is directly associated with, display

Course objectives

The students will get hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory.

Syllabus

• 1. NMR sample, preparation and handling
  2. Spectrometer setup 3. Spectrometer calibrations 4. Building blocks of pulse sequences 5. Programming of pulse sequences 6. Water suppression techniques 7. Homonuclear 2D experiments 8. Heteronuclear double and triple resonance experiments 9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN) 10. Data processing 11. Analysis of protein NMR spectra 12. Analysis of NMR spectra of nucleic acids

Literature

• NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info

Assessment methods (in Czech)

Presence in practical sessions at the spectrometer is required. Final examination will be based on results of individual projects.

Language of instruction

English

Further Comments

The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks.

Teacher's information

http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html

• Enrolment Statistics (recent)