It provides both a unique method for three-dimensional structure determination and a powerful new approach for studies of protein dynamics and folding. NMR methods to obtain novel insights into processes of biomolecular recognition. NMR is uniquely suited for studying molecular recognition processes because it can provide detailed information on structure, internal molecular dynamics, and hydration. In addition, we are using NMR to determine how protein dynamics is coupled to the catalytic activity of enzymes.
Protein folding is one of the central unsolved problems in structural biology.
Multi-dimensional NMR spectroscopy has proven to be a powerful approach for characterization of the structure and dynamics of unfolded states of proteins and protein folding intermediates. Such studies are providing new insights into the fundamental mechanisms of protein folding and the basic rules by which the amino acid sequence codes for secondary structure. In addition, coupled with stopped flow methods, NMR provides unique opportunities for structural characterization of kinetic intermediates formed during folding. P.E. A molten globule intermediate formed early on the kinetic folding pathway of apomyoglobin. Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features.