Brian W. Matthews

Our laboratory uses x-ray crystallography, in concert with other techniques, to address some of the fundamental problems in biology: how do proteins spontaneously fold into their biologically active three-dimensional configurations? what determines the stability of these folded proteins? can stability be improved? how do proteins interact with each other? how do proteins interact with DNA? how do enzymes interact with their substrates and act as catalysts? We are using the lysozyme from bacteriophage T4 to define the contributions that different types of interaction (e.g., hydrogen-bonds, hydrophobic interactions, salt bridges) make to the stability of proteins. We also are interested in the structural basis of DNA-protein recognition. Other areas of interest focus on the structure and function of peptidases and glycosidases.