Assistant Professor
B.A., History, Miami
University, 1994
Ph.D., Chemistry, Purdue
University, 2000
Postdoctoral
research, Biological Sciences, Purdue University, 2004
Room: 201B Simons Labs
Phone: (785) 864-3405
Fax: (785) 864-5736
Email: laurencej@ku.edu
Protein Structure and Function
Our lab utilizes a variety of biophysical techniques including high-field multidimensional solution NMR to determine structures and analyze dynamics of peripheral membrane proteins under various solution and environmental conditions. We examine the stability and dynamic motions of proteins and correlate these properties with efficiency of enzymatic function.
Structural studies have largely been carried out on globular proteins composed of regular secondary structure elements, and detailed information derived from these well-behaved macromolecules has contributed to our fundamental understanding of protein folds, enzyme catalysis and ligand binding. With the advent of high-throughput screening methods it has become apparent that numerous proteins involved in signal transduction have large segments that lack a globular fold, appearing disordered in the absence of their cellular context. These seemingly disordered regions interact with other proteins, nucleotides and membranes, transmitting vital information pertaining to all aspects of cell maintenance. In several proteins disorganized regions have been shown to develop specific structure in the context of binding partners. It is likely that common modes of binding exist and that new structural elements will be elucidated as these proteins are examined in the appropriate context. We are investigating the structural and functional changes that occur within proteins between the soluble and membrane bound states using a variety of biophysical, biochemical and analytical methods, including multidimensional NMR, analytical ultracentrifugation, CD and calorimetry.
