Folding units govern the cytochrome c alkaline transition

被引：95

作者：

Hoang, L ^{[1
]}

Maity, H ^{[1
]}

Krishna, MMG ^{[1
]}

Lin, Y ^{[1
]}

Englander, SW ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Biochem & Biophys, Johnson Res Fdn, Philadelphia, PA 19104 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2003年 / 331卷 / 01期

基金：

美国国家卫生研究院;

关键词：

protein folding; cytochrome c; alkaline transition; hydrogen exchange; protein function;

D O I：

10.1016/S0022-2836(03)00698-3

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 alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways. (C) 2003 Elsevier Ltd. All rights reserved.

引用

页码：37 / 43

页数：7

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