Gregory Petsko Biography

My research is concerned with the three-dimensional structures of proteins and their biochemical functions. Most of my work is done in collaboration with Prof. Dagmar Ringe; we share facilities students and a number of projects. The tools used by our group are X-ray crystallography molecular biology (especially site-directed mutagenesis) yeast genetics organic synthesis enzyme kinetics and molecular dynamics calculations. These methods are being applied to several general problems; the ones I am most involved with include: the structural basis for efficient enzymic catalysis of proton and hydride transfer; the role of the metal ions in bridged bimetalloenzyme active sites; direct visualization of proteins in action by time-resolved protein crystallography; the evolution of new enzyme activities from old ones; and the biology of the quiescent state in eukaryotic cells.
figure1In some of these projects we are trying to understand the structural basis for the catalytic power of the enzymes triose phosphate isomerase xylose isomerase mandelate racemase aminopeptidase mutarotase and ketosteroid isomerase. For all of them structural information is being used to guide site-directed mutagenesis of the active site residues and combined quantum mechanics/molecular mechanics simulations of the catalytic reaction.

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