Biomolecular NMR: Protein Dynamics and Binding

Catalog description

Prerequisites: 16268 Protein Chemistry: Principles and enrollment in 02230 Biomolecular NMR: Structure and Molecular Recognition. NMR spectroscopy is one of the most powerful tools of contemporary structural biology. Multiple NMR applications enable structural, thermodynamic, and kinetic analysis of proteins and nucleic acids under physiological conditions with site-specific resolution. The course “Biomolecular NMR: Protein Dynamics and Binding” discusses applications of NMR to protein dynamics, conformational transitions, and ligand binding. The topics include NMR line shape analysis and spin relaxation methods that are used to extract structural, thermodynamic, and kinetic parameters of conformational transitions and ligand binding in proteins. The course is directed to students who would like to utilize NMR spectroscopy as a part of the dissertation research.