Cunning simplicity of protein folding landscapes

Funnel-like landscapes are widely used to visualize protein folding. It might seem that any funnel-like energy landscape helps to avoid the `Levinthal paradox', i.e. to avoid sampling the impossibly large number of conformations for a folding protein. This cunning suggestion, reinforced by beau...

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Bibliographic Details
Published in:Protein engineering 2001-08, Vol.14 (8), p.521-523
Main Authors: Bogatyreva, Natalya S., Finkelstein, Alexei V.
Format: Article
Language:English
Subjects:
co-existence of the native and the unfolded phases
folding nucleus
Kinetics
Models, Chemical
Protein Folding
rate of folding
thermodynamic mid-transition
Thermodynamics
transition state
two-state kinetics
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Summary:Funnel-like landscapes are widely used to visualize protein folding. It might seem that any funnel-like energy landscape helps to avoid the `Levinthal paradox', i.e. to avoid sampling the impossibly large number of conformations for a folding protein. This cunning suggestion, reinforced by beautiful drawings of the energy funnels, stimulated some simple models of protein folding; one of them [D.J. Bicout and A. Szabo (2000) Protein Sci., 9, 452–465] is especially straightforward and instructive. A thorough analysis of this strict funnel model (which does not consider a nucleation of phase separation in the course of folding) shows that it cannot provide a simultaneous explanation for both major features observed for protein folding: (i) folding within non-astronomical time, and (ii) co-existence of the native and the unfolded states during the folding process. On the contrary, the nucleation mechanism of protein folding can account for both these major features simultaneously.
ISSN:0269-2139
1741-0126
1460-213X
1741-0134
DOI:10.1093/protein/14.8.521