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Science 22 February 2002:
Vol. 295. no. 5559, pp. 1480 - 1481
DOI: 10.1126/science.1069823
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Perspectives

ENZYMOLOGY:
A Moving Story

Joseph J. Falke

Many protein structures are known with high accuracy, but much less is known about their dynamics. In his Perspective, Falke highlights the report by Eisenmesser et al., who have used a nuclear magnetic resonance approach to follow protein transition state movements during catalysis in the enzyme cyclophilin A. The method should generate a wealth of new information about motions in working enzymes.

The author is in the Molecular Biophysics Program and the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. E-mail: falke{at}colorado.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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J. Camps, O. Carrillo, A. Emperador, L. Orellana, A. Hospital, M. Rueda, D. Cicin-Sain, M. D'Abramo, J. L. Gelpi, and M. Orozco (2009)
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Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems.
M. H.M Olsson, J. Mavri, and A. Warshel (2006)
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