Syllabus
1. Protein structure basics (structural motifs, protein folding, structure and function relationship, methods of 3D structure determination, protein structure database)
2. Introduction to X-ray crystallography (history, principal of the method and steps in macromolecular structure determination, sources and preparation of macromolecules for structural analysis)
3. Macromolecular crystals, their properties and preparation (theory of the crystal, symmetry, space groups, methods of macromolecular crystallization)
4. Diffraction theory (diffraction on crystal, Bragg's law, Evald construction, structure factors)
5. Data collection (X-ray sources, detectors, preparation of crystal for data collection, cryocrystallography, data collection strategies, data processing, computer programs used for data processing)
6. Structure solution, phase problem (theory of phase problem in protein crystallography, methods of phase determination)
7. Model building, refinement and model validation (electron density maps and their interpretation, stereochemical quality validation of the model)
8. Visit to protein crystallography laboratory ( visit of the department of Gene Manipulations, Institute of Molecular Genetics, Academy of the Sciences of the Czech Republic)
9. Introduction to NMR spectroscopy (basic terms, origin of NMR signal and it's processing, NMR parameters, simple pulse sequences, spin echo, polarization transfer...)
10. Methods of multidimensional NMR spectroscopy ( homonuclear and heteronuclear correlation experiments, classical versus inverse detection of NMR signal, spin-lock)
11. NMR spectroscopy of biologically active materials (structure and dynamics of proteins, oligonucleotides and saccharides, computational methods for processing experimental NMR data)
12. Using NMR spectroscopy for study of non-covalent interactions between molecules (NMR methods for characterization of complexes)
Annotation
The course will introduce basic principles of protein and nucleic acids structures. The two most often used methods of macromolecular 3D structure determination, X-ray crystallography and nuclear magnetic resonance (NMR), will be discussed in detail. The course will be supplemented with visits to laboratories using these methods.
Lectures - in Czech -