Course Identification

This course is given for Chemistry and Life Sciences Students. The aim of the course is to give an overview of the application of NMR for determining the three dimensional structure of proteins and for studying protein-ligand and protein-protein interactions. Topics to be covered: Basic principles of NMR (short introduction), two dimensional (2D) NMR techniques, sequential assignment of peptides and proteins, determination of the secondary structure of proteins, use of 3D and 4D NMR techniques for larger proteins, structure calculation, transferred NOE and other techniques for studying protein/ligand interactions, hydrogen exchange techniques and their application for studying protein folding and most recent advanced NMR methodologies for studying protein structure.

Upon successful completion of this course students should be able to:

1. Critically read and review current literature which describes the use of NMR for structural studies of proteins and their interactions with ligands.
2. Understand the capabilities and limitations of NMR in studying the structure of proteins in solution and its advantages and disadvantages over X-ray crystallography.

1. Kurt Wuthrich, NMR of Protein and Nucleic Acids
2. G.C.K. Roberts NMR of Macromolecules, A Practical Approach
3. An NMR Primer for Life Scientists
4. Jeremy N. S. Evans, Biomolecular NMR Spectroscopy
5. Protein NMR Techniques, Methods in Molecular Biology Vol 60 1997 edited by David G. Reid