The native-state ensemble of proteins provides clues for folding, misfolding and function

被引：23

作者：

Cremades, Nunilo

Sancho, Javier

Freire, Ernesto ^{[1
]}

机构：

[1] Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA

[2] Univ Zaragoza, Dept Biochem, E-50009 Zaragoza, Spain

[3] Univ Zaragoza, BIFI, E-50009 Zaragoza, Spain

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2006年 / 31卷 / 09期

关键词：

D O I：

10.1016/j.tibs.2006.07.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The predominant equilibrium in proteins is not between native and unfolded states, it is between the native and multiple partially unfolded forms. Some of these partially unfolded forms can be energetically close to the native state and, therefore, have the potential to become appreciably populated. This could have an important role in protein function or misfolding diseases. The recent identification and characterization of the partially unfolded forms of apoflavodoxin furthers our understanding of their formation.

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页码：494 / 496

页数：3

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