PřF:C6770 NMR Spectr. of Biomolecules - Course Information
C6770 NMR Spectroscopy of Biomolecules
Faculty of ScienceSpring 2004
- Extent and Intensity
- 2/0/0. 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)
Mgr. Jaromír Toušek, Dr. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer) - Guaranteed by
- prof. Mgr. Lukáš Žídek, Ph.D.
Chemistry Section – Faculty of Science
Contact Person: prof. Mgr. Lukáš Žídek, Ph.D. - Prerequisites
- Familiarity with principles of quantum mechanics will be helpful but is not required.
- 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
- Biochemistry (programme PřF, M-CH)
- Biomolecular Chemistry (programme PřF, D-BCH)
- Physical Chemistry (programme PřF, D-CH)
- Physical Chemistry (programme PřF, M-CH)
- Physical Chemistry (programme PřF, N-CH)
- Course objectives
- The course will provide introduction to modern NMR techniques which can be applied to extract structural information for small and mid-size biological macromolecules - peptides, proteins, DNA and RNA oligonucleotides. Experimental procedures and computational protocols for determination of three-dimensional structures and dynamics based on NMR data will be discussed.
- Syllabus
- 1. Principles of NMR Spectroscopy I 2. Principles of NMR Spectroscopy II 3. Basic NMR Experiments 4. Protein Structure Determination I (basic strategy, sequential assignment, side-chain assignment) 5. Protein Structure Determination II (nuclear Overhauser efect and internuclear distances, three-bond scalar couplings and torsion angles, other spatial restraints) 6. Protein Structure Determination III (secondary structure determination, intermolecular complexes, large proteins and membrane proteins) 7. Nucleic Acid Structure Determination I 8. Nucleic Acid Structure Determination II 9. Structure Refinement Using Molecular Dynamics 10. Dynamics of Biomolecules I (dynamics of molecules and NMR relaxation, theory of relaxation) 11. Dynamics of Biomolecules II 12. Review
- Literature
- 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
- Assessment methods (in Czech)
- Oral examination
- Language of instruction
- English
- Follow-Up Courses
- Further Comments
- The course is taught annually.
The course is taught: every week. - Teacher's information
- http://www.ncbr.chemi.muni.cz/~lzidek/C6770.html
- Enrolment Statistics (Spring 2004, recent)
- Permalink: https://is.muni.cz/course/sci/spring2004/C6770