Our efforts in protein dynamics center on the use of high-resolution liquid and solid state NMR spectroscopy to characterize the nature of protein motion and its influence on function. Historically, we have focused on the very fast internal motions that are naturally characterized by classical NMR relaxation phenomena. This has required the development of novel isotopic labeling and multidimensional sampling methods and a variety of analytical strategies. NMR is perhaps the most ideal experimental technique for obtaining comprehensive site resolved (i.e. at atomic resolution) information. NMR relaxation studies have revealed that the internal dynamics of proteins are surprisingly rich. We have discovered that motion on the side chains is generally much more varied than on the backbone. We are currently interested in understanding the physical origins and biological significance of these motions. A critical product of these studies is the quantitative interpretation of changes in motion as changes in conformational entropy, a previously experimentally inaccessible quantity.

For more detailed information click here.