Biomolecular NMR of Protein Assemblies: Theory and Applications

Catalog description

Solid-state NMR (ssNMR) is a unique technology to study the structure and dynamics of insoluble biomacromolecules in the rigid or semi-rigid forms, such as, membrane proteins, amyloid fibrils, sedimented proteins, and cellular extracts. The course starts with a brief introduction to solution and solid-state NMR spectroscopy with applications ranging from small molecules to macromolecular protein assemblies. We will then work on the NMR spin physics using product operator formalism and average Hamiltonian theory. Basic building blocks of ssNMR experiments consist of polarization transfer between different nuclei. These building blocks will be used to construct triple resonance multi-dimensional experiments for protein analysis. Recent methodological and technological advancements for pushing the limits of sensitivity and resolution will be summarized. Sample conditions and protein dynamics play a significant role in the selection of ssNMR experiments. Several examples from the protein ssNMR literature will be discussed to understand various aspects of sample preparation and NMR probe technology. Example data sets and NMR software (TOPSPIN) will be provided to get hands on experience on data processing.