Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain

被引：11

作者：

Jemth, Per ^{[1
]}

Johnson, Christopher M. ^{[1
]}

Gianni, Stefano ^{[1
]}

Fersht, Alan R. ^{[1
]}

机构：

[1] MRC, Ctr Prot Engn, Cambridge CB2 2QH, England

来源：

PROTEIN ENGINEERING DESIGN & SELECTION | 2008年 / 21卷 / 03期

基金：

英国医学研究理事会;

关键词：

FF domain; stopped-flow spectrometry; burst-phase analysis; kinetics; protein folding;

D O I：

10.1093/protein/gzm091

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 role of intermediates in the folding reaction of single-domain proteins is a controversial issue. It was previously shown by different methods that an on-pathway intermediate is populated in the presence of sodium sulphate during the folding of the FF domain from HYPA/FBP11. Here we demonstrate using analysis of the amplitudes of kinetic traces that this burst-phase folding intermediate is present at different salt concentration and at various pH, and is also found in roughly 30 site-directed mutants. The intermediate appears robust to changing conditions and thus fulfils an important criterion for a productive molecular species on the folding reaction pathway.

引用

页码：207 / 214

页数：8

共 36 条

[1] Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c [J].