Nuclear Magnetic Resonance in Structural Biology - Alessandro Pintar, Protein Structure and Bioinformatics, ICGEB, Trieste
Thanks to advancements both in the
theory and in the instrumentation, Nuclear Magnetic Resonance (NMR) has widened its use from small organic molecules to oligosaccharides, peptides, proteins, and nucleic acids. Together with X-ray crystallography, NMR is the only technique that can provide structural information at the atomic level. However, applications of NMR are not limited to 3D structure calculation: it can be used to study flexible biomolecules (peptides, oligosaccharides, small nucleic acids) that cannot be crystallized, unfolded or partially folded proteins, ligand/protein interactions, and to get insight into the electrostatics and the internal dynamics of proteins. Promising applications include the structure determination of membrane proteins by solid-state NMR.
This lecture is intended to provide biologists with the basic concepts of modern biomolecular NMR, the technical background necessary to understand structural biology work based on NMR, and practical hints for those who are planning to use NMR to address biological problems.