Motional Modelling by NMR

Regents Of The University Of Michigan - Ann Arbor, Ann Arbor MI

Investigators

Abstract

This research will investigate protein dynamics in detail in order to understand how these macromolecules, especially enzymes, precisely work. Nuclear Magnetic Resonance Spectroscopy has proven over the years to be a viable method to determine protein dynamics. But, it has mostly been limited to the determination of the motions of the NH vector in proteins. In this project, the dynamical processes of many different vectors in proteins using residual dipolar couplings experiments, conformational exchange broadening experiments and cross-correlated relaxation measurements will be investigated. To interpret these data, theoretical computations of the chemical shift tensors will also be carried out. All these data will be combined to formulate comprehensive dynamical models of anisotropic local motion that are important for the complete description of the protein's molecular and energetic properties. Proteins are not nearly as static as is often assumed. The molecules have intrinsically mobile areas which are necessary to perform diverse functions in a living cell. Nuclear magnetic resonance spectroscopy is a technique that can retrieve the dynamical properties of virtually each atom, individually, in a biological macromolecule, such as protein. The detailed insights will likely help in the fundamental understanding of the molecules of life.