X-Ray Crystallographic Analysis of Protein-Ligand Interactions
Mark earned his PhD in 1991 from Yale, where he solved the first molecular structure of a tRNA synthetase bound to its cognate tRNA, in Tom Steitz’ lab. During his post-doc with Prof Carl Pabo at MIT, he participated in the x-ray crystallographic determination of more than a dozen macromolecular structures, primarily protein-DNA complexes. Mark joined UVM in 1998 to create the Center for X-Ray Crystallography and serve as its first director.
We develop and apply x-ray crystallographic and computational methods to better detect, analyze and optimize the binding of small molecules to target proteins. When optimized for their affinity to a chosen target, these small molecules serve as the starting point, or lead compounds, for pharmaceutical design. Our emphasis is on developing protocols for the rapid identification of lead compounds to challenging targets, such as to protein surfaces that interface with other macromolecules.
Rould, M.A., Carter, C.W. Jr. (2003) Isomorphous Difference Methods Methods in Enzymology 374, 145-163
Wally J, Halbrooks PJ, Vonrhein C, Rould MA, Everse SJ, Mason AB, Buchanan SK. (2006) The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding J. Biol. Chem. 281, 24934-44
Rould M.A, Wan Q., Joel P.B., Lowey S., Trybus K.M. (2006) Crystal Structures of Expressed Non-polymerizable Monomeric Actin in the ADP and ATP States J Biol Chem,in press [Epub:doi:10.1074/jbc.M601973200]
* indicates equal contribution
Department of Molecular Physiology & Biophysics
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