Serpin Structure, Mechanism, and Function

Peter G. W. Gettins*
Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, M/C 536, 1819-53 West Polk Street, Chicago, Illinois 60612
Chem. Rev., 2002, 102 (12), pp 4751–4804
DOI: 10.1021/cr010170+
Publication Date (Web): November 8, 2002
Copyright © 2002 American Chemical Society
*

 Correspondence address:  Department of Biochemistry & Molecular Genetics, M/C 536, 1819-53 West Polk Street, Chicago, IL 60612. E-mail:  pgettins@uic.edu.

Peter G. W. Gettins was born in Sunderland, UK, in 1953 and became a U.S. citizen in 1990. He received his M.A. in chemistry (1976) and D.Phil. in biochemistry (1979) from Oxford University. Work for his doctoral thesis, under the guidance of Raymond A. Dwek, was on the application of NMR to antibody combining sites. After postdoctoral work at Yale University under the supervision of Joseph E. Coleman, applying multinuclear NMR to the study of the metalloenzyme alkaline phosphatase, he took a position as Assistant Professor in the Department of Biochemistry at Vanderbilt University in 1984. In 1988, he was appointed Associate Professor and in 1993 moved to the Department of Biochemistry at the University of Illinois at Chicago as Professor. He is also currently the Interim Director of the Center for Structural Biology at the University of Illinois at Chicago. His research interests are in the structure and function of the superfamily of proteins known as serpins and of the low-density lipoprotein receptor-related protein (LRP) which binds and clears serpin-proteinase complexes and many other unrelated protein ligands. His laboratory uses a range of biophysical and biochemical approaches in these studies, including NMR and fluorescence spectroscopies, X-ray crystallography, calorimetry, and kinetic analysis.

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