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Issue 1, 2009
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Collapse transition in proteins

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The coil–globule transition, a tenet of the physics of polymers, has been identified in recent years as an important unresolved aspect of the initial stages of the folding of proteins. We describe the basics of the collapse transition, starting with homopolymers and continuing with proteins. Studies of denatured-state collapse under equilibrium are then presented. An emphasis is placed on single-molecule fluorescence experiments, which are particularly useful for measuring properties of the denatured state even under conditions of coexistence with the folded state. Attempts to understand the dynamics of collapse, both theoretically and experimentally, are then described. Only an upper limit for the rate of collapse has been obtained so far. Improvements in experimental and theoretical methodology are likely to continue to push our understanding of the importance of the denatured-state thermodynamics and dynamics for protein folding in the coming years.

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The article was received on 12 Aug 2008, accepted on 13 Oct 2008 and first published on 14 Nov 2008

Article type: Perspective
DOI: 10.1039/B813961J
Phys. Chem. Chem. Phys., 2009,11, 83-93

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    Collapse transition in proteins

    G. Ziv, D. Thirumalai and G. Haran, Phys. Chem. Chem. Phys., 2009, 11, 83
    DOI: 10.1039/B813961J

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