C5846 Advanced Biophysical Chemistry - experimental methods

Faculty of Science
Spring 2019
Extent and Intensity
2/1/0. 3 credit(s) (plus extra credits for completion). Type of Completion: zk (examination).
Teacher(s)
prof. RNDr. Libuše Trnková, CSc. (lecturer)
doc. RNDr. Mgr. Jozef Hritz, Ph.D. (lecturer)
doc. Mgr. Zdeněk Farka, Ph.D. (lecturer)
RNDr. Mgr. Iveta Třísková, Ph.D. (lecturer)
Mgr. Jan Novotný, Ph.D. (lecturer)
prof. RNDr. Zbyněk Prokop, Ph.D. (lecturer)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
doc. Mgr. Pavel Plevka, Ph.D. (lecturer)
Mgr. Tomáš Klumpler, Ph.D. (lecturer)
Guaranteed by
prof. RNDr. Libuše Trnková, CSc.
Department of Chemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Chemistry – Chemistry Section – Faculty of Science
Prerequisites
Successful passing the courses: C5850 - Principles of Biophysical Chemistry (lecture) C5855 - Methods of Biophysical Chemistry (lecture) C5856 - Methods of Biophysical Chemistry (seminar)
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
Course objectives
The aim of this subject is to gain deeper knowledge of biophysical chemistry for its application in the study of biomolecules. The emphasis is put not only at the physico-chemical principles of a variety of biophysical experimental methods and their applications in biomolecular systems but also at new knowledge in the modern techniques.
Learning outcomes
Students will be able: - to describe biopolymer systems using modern experimental biophysical methods; - to apply physicochemical experimental approaches to solve the relationship between the structure and function of biologically important molecules; - to evaluate critically the applicability of many experimental methods to describe dynamic changes in biomolecular systems under study.
Syllabus
  • 1. Chemical conditions for the study of bio-macromolecules and molecular complexes (pH, solvent, buffer, ionic strength, temperature, radiation) 2. Chromatography (physical and chemical principles of various chromatographic techniques, the meaning of purification protocols for nucleic acids and proteins) 3. Spectroscopic methods (variety of spectroscopic techniques, importance for the characterization of biomolecules and for the study of their behavior in solutions) 4. Mass spectrometry (the physical basis, techniques, applications, the possibility to connect the technique with other high resolution techniques, the application in the study of proteins, peptides and NA) 5. Electrophoresis (physical basics of the method, types, its range of application in research of biomolecules, the technique can be interfaced with other sensitive techniques, applications for proteins and NAs research) 6. Diffraction method (X-ray diffraction experiments, studies of structures and structural changes of proteins, nucleic acids and their complexes) 7. Bio-calorimetry (the physical meaning of the thermodynamic parameters, types of calorimetric techniques, studying the structures of biomolecules and their interactions in solutions) 8. Bioelectrochemistry (types of electrochemical techniques, their principles, electrochemistry DNAs and RNAs, proteins and their components, biosensors, electrode systems, electron transfer and electron-proton transfer) 9. Hydrodynamic methods (the principles of methods, viscosity, sedimentation, centrifugation, filtration, dialysis and cytometry; the study of biomolecules, viruses, cells) 10. Size and shape of macromolecules (molecular electron microscopy, microscopic image, translation and rotation frictional properties) 11. Macromolecular diffusion (molecular interpretation of diffusion, mass transport as flux, diffusion in multicomponent systems) 12. Bioinformatics (the main three-dimensional structure available via the www pages, overviews of the structure data, information and extract operationally relevant data, modeling of structures and their drawbacks) Literature: [1] Peter R. Bergethon: The Physical Basis of Biochemistry [2] Finkelstein and Pittsyn: Protein Physics [3] Cantor & Schimmel: Biophysical Chemistry, Part II and III [4] Zuckerman D.M.: Statistical Physics of Biomolecules
Literature
    recommended literature
  • CANTOR, Charles R. and Paul R. SCHIMMEL. Biophysical chemistry. Part II, Techniques for the study of biological structure and function. 12th print. New York: W.H. Freeman and Company. xxix, s. 3. ISBN 0-7167-1189-3. 2001. info
  • CANTOR, Charles R. and Paul R. SCHIMMEL. Biophysical chemistry. Part III, The behavior of biological macromolecules. New York: W.H. Freeman and Company. xxix, s. 8. ISBN 0-7167-1191-5. 1980. info
Teaching methods
lecture (2 hours)including short excursions of the presented techniques (1 hour)
Assessment methods
oral examination and credit test
Language of instruction
Czech
Further Comments
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
The course is also listed under the following terms Spring 2017, spring 2018, Spring 2020, Spring 2021, Spring 2022, Spring 2023, Spring 2024, Spring 2025.
  • Enrolment Statistics (Spring 2019, recent)
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