Native conformational tendencies in unfolded polypeptides: Development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins

被引：6

|

作者：

Narayan, M ^{[1
]}

Welker, E ^{[1
]}

Scheraga, HA ^{[1
]}

机构：

[1] Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2003年 / 125卷 / 08期

关键词：

D O I：

10.1021/ja021252y

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

引用

收藏

页码：2036 / 2037

页数：2

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[1] Native conformational tendencies in unfolded polypeptides: Development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins
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[2] Multiple Disulfide-Bonded States of Native Proteins: Estimate of Number Using Probabilities of Disulfide Bond Formation
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[3] Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: Implications for the mechanism of oxidative folding of RNase A
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Welker, E
Narayan, M
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JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (18) : 4995 - 4999