Paul Thomas Wingfield, Ph.D.

Senior Investigator

Protein Expression Laboratory

NIAMS

Building 6B, Room 1B130
6 Center Drive
Bethesda, MD 20814

301-594-1313

wingfiep@mail.nih.gov

Research Topics

The NIAMS Protein Expression Laboratory supports intramural NIH scientists in studying the structure and function of Human Immunodeficiency Virus (HIV) proteins. Most structural biology techniques, especially those for studying the three-dimensional structures of proteins, require large quantities of highly purified, monodisperse, and correctly folded proteins. The Protein Expression Laboratory responds to this need by analyzing and providing HIV proteins to NIH and collaborating scientists. 

Biography

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

  1. Stahl SJ, Watts NR, Rader C, DiMattia MA, Mage RG, Palmer I, Kaufman JD, Grimes JM, Stuart DI, Steven AC, Wingfield PT. Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev. J Mol Biol. 2010;397(3):697-708.

  2. DiMattia MA, Watts NR, Stahl SJ, Rader C, Wingfield PT, Stuart DI, Steven AC, Grimes JM. Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element. Proc Natl Acad Sci U S A. 2010;107(13):5810-4.

  3. Jedidi I, Zhang F, Qiu H, Stahl SJ, Palmer I, Kaufman JD, Nadaud PS, Mukherjee S, Wingfield PT, Jaroniec CP, Hinnebusch AG. Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit mediator to target genes in vivo. J Biol Chem. 2010;285(4):2438-55.

  4. Watts NR, Vethanayagam JG, Ferns RB, Tedder RS, Harris A, Stahl SJ, Steven AC, Wingfield PT. Molecular basis for the high degree of antigenic cross-reactivity between hepatitis B virus capsids (HBcAg) and dimeric capsid-related protein (HBeAg): insights into the enigmatic nature of the e-antigen. J Mol Biol. 2010;398(4):530-41.

  5. Lakomek NA, Kaufman JD, Stahl SJ, Wingfield PT. HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation. Structure. 2014;22(9):1311-21.


This page was last updated on February 10th, 2010