In my laboratory, we are interested in two protein systems – the lens alpha-crystallins and the bile acid CoA:amino acid N-acyltransferases (BAATs). The alpha-crystallins act as chaperones to prevent unfolded proteins in the lens from precipitating. Using mass spectrometry imaging, we have found that alphaA-crystallin undergoes truncation at as many as 16 different sites. We now plan to examine what provides the control of truncation and is it physiologic? The goal of studies on the BAATs is to determine the structure of these hepatic enzymes by molecular modeling, X-ray crystallography, hydrogen/deuterium exchange mass spectrometry, and NMR.
Dr. Barnes received his B.S. Degree from the University of Surrey, UK; and his Ph.D. Degree from the University of London, UK. He went on to do his postdoctoral training at the Department of Chemical Pathology, St. Thomas' Hospital, London, UK and Royal Free Hospital Academic Department of Medicine, London, UK.