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Int. J. Mol. Sci. 2010, 11(12), 5292-5309; doi:10.3390/ijms11125292
Review

Intrinsically Disordered Proteins in a Physics-Based World

,  and *
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA These authors contributed equally to this work.
* Author to whom correspondence should be addressed.
Received: 19 October 2010 / Revised: 17 December 2010 / Accepted: 17 December 2010 / Published: 21 December 2010
(This article belongs to the Special Issue Advances in Molecular Recognition)
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Abstract

Intrinsically disordered proteins (IDPs) are a newly recognized class of functional proteins that rely on a lack of stable structure for function. They are highly prevalent in biology, play fundamental roles, and are extensively involved in human diseases. For signaling and regulation, IDPs often fold into stable structures upon binding to specific targets. The mechanisms of these coupled binding and folding processes are of significant importance because they underlie the organization of regulatory networks that dictate various aspects of cellular decision-making. This review first discusses the challenge in detailed experimental characterization of these heterogeneous and dynamics proteins and the unique and exciting opportunity for physics-based modeling to make crucial contributions, and then summarizes key lessons from recent de novo simulations of the structure and interactions of several regulatory IDPs.
Keywords: conformational selection; generalized Born; implicit solvent; induced folding; molecular dynamics; p21; p27; p53; pKID; replica exchange conformational selection; generalized Born; implicit solvent; induced folding; molecular dynamics; p21; p27; p53; pKID; replica exchange
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Click, T.H.; Ganguly, D.; Chen, J. Intrinsically Disordered Proteins in a Physics-Based World. Int. J. Mol. Sci. 2010, 11, 5292-5309.

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