Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution
Tatyana I. Igumenova,
† Kendra King Frederick, and A. Joshua Wand
* Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059
Chem. Rev., 2006, 106 (5), pp 1672–1699
DOI: 10.1021/cr040422h
Publication Date (Web): April 26, 2006
Copyright © 2006 American Chemical Society
† Present address: Department of Biochemistry & Biophysics, Columbia University, New York, NY 10032.
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* To whom correspondence should be addressed. Telephone: 215-573-7288. Fax: 215-573-7290. E-mail: wand@mail.med.upenn.edu.
Tatyana Igumenova was born and raised in Novosibirsk, Russia. She completed her undergraduate degree in chemistry at Novosibirsk State University. In 2003, she received her Ph.D. (with distinction) in chemistry from Columbia University for work with Ann McDermott on solid-state NMR of proteins. From 2003 to 2005, she was an NIH postdoctoral fellow with Josh Wand at the University of Pennsylvania, where she studied the role of fast side chain dynamics in long-range coupling of allosteric sites in calmodulin. She is currently an NIH postdoctoral fellow with Arthur G. Palmer, III, at Columbia University.
Kendra K. Frederick received her B.S. in French language and literature and biochemistry with honors in 2000 from the University of Michigan, where she worked with Dr. David Ballou and Dr. Bruce Palfey on the transient-state kinetics of flavoprotein reduction. She received a M.S. in 2001 from the Université de Paris XI in Orsay, France, under the direction of Dr. Florence Lederer (CNRS, Gif-sur-Yvette). She is currently pursuing a Ph.D. in biophysics in the laboratory of Josh Wand at the University of Pennsylvania, where she uses NMR relaxation techniques to investigate the role that protein dynamics play in protein−protein interactions.
Josh Wand was born and raised in Ottawa, Canada. He received his B.Sc. (honors) in biochemistry from Carleton University in Ottawa. Working under the direction of Stan Tsai, he also received a M.Sc. in bioorganic chemistry from Carleton University. He received his Ph.D. in biophysics from the University of Pennsylvania under the guidance of Walter Englander. After a short postdoctoral stint in solid-state NMR at the National Research Council of Canada with I. C. P. Smith, he joined the faculty of the Institute for Cancer Research. He subsequently spent time on the faculties of the University of Illinois at Urbana-Champaign and the State University of New York at Buffalo. He is currently the Benjamin Rush Professor of Biochemistry and chair of the graduate group in biochemistry and molecular biophysics at the University of Pennsylvania, where he continues to employ novel applications of solution NMR to questions in protein biophysics.
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