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Collapse transition in proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ziv, Guy Thirumalai, D. Haran, Gilad
Description	Country affiliation: Israel Author Affiliation: Ziv G ( Chemical Physics Department, Weizmann Institute of Science, 76100, Rehovot, Israel.)
Abstract	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.
File Format	HTM / HTML
ISSN	14639076
e-ISSN	14639084
DOI	10.1039/b813961j
Journal	Physical Chemistry Chemical Physics
Issue Number	1
Volume Number	11
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2009-01-07
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Physics Discipline Biophysics Discipline Chemistry Proteins Chemistry Fluorescence Protein Conformation Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Physics and Astronomy Physical and Theoretical Chemistry

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