Unfolded, yes, but random? Never!

被引：81

作者：

Plaxco, KW ^{[1
]}

Gross, M

机构：

[1] Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA

[2] Oxford Ctr Mol Sci, Cent Chem Lab, Oxford OX1 3QH, England

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 08期

关键词：

D O I：

10.1038/90349

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：

NMR experiments with partially aligned protein molecules in strongly denaturing conditions suggest that the unfolded state is less chaotic than is widely believed. Hence protein folding is probably less paradoxical than Levinthal originally thought.

引用

页码：659 / 660

页数：2

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