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Research
Protein Expression Laboratory
Senior Investigator
Phone: 301-594-1313
Building: 6B, Room: 1B130
E-mail: wingfiep@mail.nih.gov
Dr. Wingfield, a native of Great Britain, has directed the Protein Expression Laboratory since its inception in 1989. In 1997, he received the NIH Director's Award for designing and establishing the Laboratory. Previously, Dr. Wingfield was department head of protein chemistry at Glaxo Institute for Molecular Biology (formerly Biogen SA) in Geneva, Switzerland, where he spent nine years perfecting and using techniques for the production of recombinant protein and their structural characterization. Earlier, he was a staff scientist in the biological structures division of the European Molecular Biology Laboratory, Heidelberg, Germany. Dr. Wingfield received his doctorate from Dundee University in Scotland and was a postdoctoral scholar in biological chemistry at the University of California, Los Angeles. Dr. Wingfield has published more than 100 articles in national and international scientific journals, among them the majority of those cited with the lab selected publications.
Selected Publications
Sergeev YV, Hejtmancik JF, Wingfield PT. Energetics of domain-domain interactions and entropy driven association of beta-crystallins. Biochemistry. 2004; 43(2): 415-24
Davis DA, Brown CA, Newcomb FM, Boja ES, Fales HM, Kaufman J, Stahl SJ, Wingfield P, Yarchoan R. Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation. J Virol. 2003; 77(5): 3319-25.
Conway JF, Watts NR, Belnap DM, Cheng N, Stahl SJ, Wingfield PT, Steven AC. Characterization of a conformational epitope on hepatitis B virus core antigen and quasiequivalent variations in antibody binding. J Virol. 2003; 77(11): 6466-73.
Belnap DM, Watts NR, Conway JF, Cheng N, Stahl SJ, Wingfield PT, Steven AC. Diversity of core antigen epitopes of hepatitis B virus. Proc Natl Acad Sci U S A. 2003; 100(19):10884-9.
Davis DA, Newcomb FM, Moskovitz J, Wingfield PT, Stahl SJ, Kaufmann S, et al. HIV-2 Protease is inactivated following oxidation at the dimer interface and activity can be restored with methionine sulfoxide reductase. Biochem J. 2000; 346: 305-11.
