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Titolo:
Cunning simplicity of protein folding landscapes
Autore:
Bogatyreva, NS; Finkelstein, AV;
Indirizzi:
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142290 cow Region, Russia Samara State Univ, Dept Math, Samara 443086, Russia Samara State Univ Samara Russia 443086 Dept Math, Samara 443086, Russia
Titolo Testata:
PROTEIN ENGINEERING
fascicolo: 8, volume: 14, anno: 2001,
pagine: 521 - 523
SICI:
0269-2139(200108)14:8<521:CSOPFL>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
LATTICE MODEL; KINETICS; FUNNELS; PARADOX;
Keywords:
co-existence of the native and the unfolded phases; folding nucleus; protein folding; rate of folding; thermodynamic mid-transition; transition state; two-state kinetics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
18
Recensione:
Indirizzi per estratti:
Indirizzo: Finkelstein, AV Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142290 ia
Citazione:
N.S. Bogatyreva e A.V. Finkelstein, "Cunning simplicity of protein folding landscapes", PROTEIN ENG, 14(8), 2001, pp. 521-523

Abstract

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 andthe unfolded states during the folding process. On the contrary, the nucleation mechanism of protein folding can account for both these major features simultaneously.

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Documento generato il 04/12/20 alle ore 20:00:32