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. Students who finish the course successfully will understand principles of NMR and its applications to biochemical problems described in original research articles, to analyze NMR experiments and design their modification, to chose the correct approach of solving a given problem, and to combine results of individual approaches to obtain a complex picture of the studied problem. The course is designed so that students who continue to study in a PhD program will be able to apply the learned skills in their own research projects.
1. NMR as a tool for structure biology
2. Basic NMR Experiments
3. Key to biomolecular NMR: Idea of correlation
4. First step in NMR of proteins
5. Second step in determination of protein structure
6. From spectra to structure
7. Special features of nucleic acid NMR
8. Nucleic acid structure by NMR
9. Molecules are not rigid
10. From relaxation to molecular motions
11. Molecules are not alone
12. Beyond small soluble biomolecules
CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007. xxv, 885. ISBN 9780121644918. info
Lectures combining explanation of basic ideas with analysis of model examples, computer simulations of the discussed topics.
Oral examination in a form of discussion of problems solved by the student.