Syllabus
1. Comparison of techniques used to study structure of biopolymers.2. Protein crystallization, symmetry, crystal systems, Bravais lattices, unit cell, asymmetric unit.3. Theory of diffraction. Atomic scattering factor. Structural factor.4. Laue conditions. Reciprocal lattice. Ewald construction. Phase problem.
5. Methods of phase problem solution. Patterson map and identification of heavy atom locations. Principles of MIR, SIR, SAD, MAD and MR.6. Collection and processing of diffraction data. Model building. Structure refinement. Analysis of obtained structural model.7. Principle of NMR, 2D NMR. COSY and NOESY. Protein NMR.
8. Cryo-electron microscopy.9. Analytical ultracentrifugation. Sedimentation velocity and sedimentation equilibrium methods.10. Microcalorimetry. ITC and DSC.11. Surface plasmon resonance (SPR).12. SAXS - small angle X-ray scattering.13. Selected techniques of mass spectrometry (chemical cross-linking, HDX-MS).
Annotation
BIOPHYSICAL CHEMISTRY II
The objective of the course is to provide a deep understanding of physical chemistry applied to biological problems in order to understand structure and function. The course should make the student familiar with the most important methods of studying and interpreting protein structure and function (protein x-ray crystallography, SAXS, NMR, cryo-EM, ITC and DSC, SPR, analytical ultracentrifugation and selected methods of mass spectrometry).