Metastability of Native Proteins and the Phenomenon of Amyloid Formation

被引：326

作者：

Baldwin, Andrew J. ^{[1
]}

Knowles, Tuomas P. J. ^{[1
]}

Tartaglia, Gian Gaetano ^{[1
]}

Fitzpatrick, Anthony W. ^{[1
]}

Devlin, Glyn L. ^{[1
]}

Shammas, Sarah Lucy ^{[1
]}

Waudby, Christopher A. ^{[1
]}

Mossuto, Maria F. ^{[1
]}

Meehan, Sarah ^{[1
]}

Gras, Sally L. ^{[2
]}

Christodoulou, John ^{[3
]}

Anthony-Cahill, Spencer J. ^{[4
]}

Barker, Paul D. ^{[1
]}

Vendruscolo, Michele ^{[1
]}

Dobson, Christopher M. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

[2] Univ Melbourne, Dept Chem & Biomol Engn, Parkville, Vic 3010, Australia

[3] UCL, Dept Struct & Mol Biol, London WC1E 6BT, England

[4] Western Washington Univ, Dept Chem, Bellingham, WA 98225 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2011年 / 133卷 / 36期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金; 英国工程与自然科学研究理事会;

关键词：

FIBRILS;

D O I：

10.1021/ja2017703

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions. This result challenges the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces and suggests that living systems are conformationally as well as chemically metastable.

引用

页码：14160 / 14163

页数：4

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