Fast Time Scale Dynamics of Protein Backbones:  NMR Relaxation Methods, Applications, and Functional Consequences

Virginia A. Jarymowycz and Martin J. Stone*
Department of Chemistry and Interdisciplinary Biochemistry Program, Indiana University, Bloomington, Indiana 47405-0001
Chem. Rev., 2006, 106 (5), pp 1624–1671
DOI: 10.1021/cr040421p
Publication Date (Web): April 25, 2006
Copyright © 2006 American Chemical Society
*

 Author to whom correspondence should be addressed [telephone (812) 855-6779; fax (812) 855-8300; e-mail mastone@indiana.edu].

Virginia A. Jarymowycz (née Goehlert) received her B.S. degree in biochemistry from Indiana University in 2001. She is currently pursuing a Ph.D. through the Interdisciplinary Biochemistry Program at Indiana University in the laboratory of Dr. Martin J. Stone. Her thesis research is focused on using NMR relaxation techniques to investigate the potential contributions of fast time scale dynamics to observed protein stability and function.

Martin J. Stone received his B.Sc. and M.Sc. (honors) degrees (in 1986 and 1987, respectively) from the University of Auckland (New Zealand) and his Ph.D. degree in 1991 from the University of Cambridge (United Kingdom), where he studied with Prof. Dudley H. Williams. He performed postdoctoral research with Prof. Peter Wright at the Scripps Research Institute (La Jolla, CA) and then joined the Department of Chemistry and Program in Biochemistry at Indiana University, Bloomington, IN. His research spans two major areas:  understanding the relationships of protein dynamics to structure, stability, and function and studying the structural basis of receptor recognition by chemokine proteins.

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History

  • Published In Issue May 10, 2006
  • Received January 7, 2005

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