PROTEIN-FOLDING INTERMEDIATES - NATIVE-STATE HYDROGEN-EXCHANGE

被引：1006

作者：

BAI, YW ^{[1
]}

SOSNICK, TR ^{[1
]}

MAYNE, L ^{[1
]}

ENGLANDER, SW ^{[1
]}

机构：

[1] UNIV PENN, SCH MED, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA

来源：

SCIENCE | 1995年 / 269卷 / 5221期

关键词：

D O I：

10.1126/science.7618079

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.

引用

页码：192 / 197

页数：6

共 43 条

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