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Published online before print June 17, 2008, 10.1110/ps.03259908
Protein Science (2008), 17:1295-1307. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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REVIEW

Allostery and cooperativity revisited

Qiang Cui1 and Martin Karplus2,3

1 Department of Chemistry and Theoretical Chemistry Institute, University of Wisconsin, Madison, Wisconsin 53706, USA
2 Laboratoire de Chimie Biophysique, ISIS Université Louis Pasteur, 67000 Strasbourg, France
3 Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA

(RECEIVED September 25, 2007; FINAL REVISION September 25, 2007; ACCEPTED December 4, 2007)

Although phenomenlogical models that account for cooperativity in allosteric systems date back to the early and mid-60's (e.g., the KNF and MWC models), there is resurgent interest in the topic due to the recent experimental and computational studies that attempted to reveal, at an atomistic level, how allostery actually works. In this review, using systems for which atomistic simulations have been carried out in our groups as examples, we describe the current understanding of allostery, how the mechanisms go beyond the classical MWC/Pauling-KNF descriptions, and point out that the "new view" of allostery, emphasizing "population shifts," is, in fact, an "old view." The presentation offers not only an up-to-date description of allostery from a theoretical/computational perspective, but also helps to resolve several outstanding issues concerning allostery.

Keywords: conformational change; MWC; Pauling-KNF; allostery; protein dynamics


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