Molecular biophysics II 1101-519
The aim of this course is description of selected problems of molecular biophysics, and to make acquainted with biophysics as a one of the division of physics. Theoretical and experimental background of molecular biophysics will be explained. Some lectures illustrate the scope and limitations of physics in studies of biological systems.
Program:
1. Theoretical basis of relaxation methods.
2. Review of basic experimental techniques of relaxation methods (T-jump, E-field jump, stopped-flow spectrometry, laser flash photolysis) with presentation of selected problems in biophysics of proteins and nucleic acids.
3. Application of molecular modeling and computer simulations to analysis of results of experiments employing relaxation methods.
4.Crystallization of proteins - factors affecting protein solubility, nucleation and crystal growth; phase diagram; commonly used precipitants; crystallization methods: sitting and hanging drop, dialysis, micro- and macro-seeding; "screens", quality of protein crystals; resolution.
5.Protein crystallography - physical and theoretical basis; experimental techniques, X-ray sources and detectors; stages of solving the X-ray structure, problems associated with each stage, phase problem; resolution; time-resolved crystallography.
6. Nuclear magnetic resonance in biology and medicine.
a) Spectroscopic investigations of intact cell and tissue metabolism (in vivo NMR).
b) Magnetic resonance imaging (MRI) of living organisms; combination with in vivo NMR.
c) Studies of biological membranes: broad line NMR and cross-polarization magic angle spinning (CPMAS).
7. Theoretical background of photophysics of biomolecules.
8. Techniques and methods of modern emission spectroscopy of biomolecules.
9. Excited-state lifetime and interpretation of fluorescence intensity decays.
10. Interpretation of steady-state and time-resolved fluorescence anisotropy.
11. Non-radiative quenching of excited states by intra- and intermolecular phenomena.
12. Simultaneous absorption of two photons - similarities and differences between fluorescence induced by one- and multi-photon absorption.
13. Emission methods in microscopy, and in medical diagnosis (structural imaging of cells and tissues).
14. Structural and physical properties of biomolecules derived from circular dichroism (CD), IR absorption and Raman scattering.
Description by Borys Kierdaszuk, November 2010.
Type of course
Prerequisites
Bibliography
1. C.R. Cantor i P.R. Schimmel, Biophysical Chemistry, W.H. Freeman and Co., New York, Part I-III, 1980.
2. C.F. Bernasconi, Relaxation Kinetics, Academic Press, New York, 1976.
3. J.A. McCammon , S. Harvey, Dynamics of Proteins and Nucleic Acids. Cambridge University Press, Cambridge, 1987.
4. K. Wuthrich, NMR in Biological Research: Peptides and Proteins. North-Holland, Amsterdam, 1976.
5. J.R. Lakowicz, Principles of Fluorescence Spectroscopy. 3rd edition, Springer-Verlag, 2006.
6. A. Kawski, Photoluminescence of Solutions, (in polish) PWN, Warsaw, 1992.
7. A.R. Fersht, Enzyme Structure and Mechanism. W. H. Freeman and Company, San Francisco, 1985.
8. W. Saenger, Principles of Nucleic Acid Structure. Springer-Verlag, New York and Berlin, 1984.
9. D.E. McRee, Practical Protein Crystallography, 2nd edition, Academic Press, San Diego, 1999.
10. J. Drenth, Principles of Protein X-Ray Crystallography. 3nd edition, Springer-Verlag, New York, 2006.
Additional information
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