Cytochrome c folding pathway:: Kinetic native-state hydrogen exchange

被引：112
|
作者：
Hoang, L [1 ]
Bédard, S [1 ]
Krishna, MMG [1 ]
Lin, Y [1 ]
Englander, SW [1 ]
机构：
[1] Univ Penn, Sch Med, Johnson Res Fdn, Philadelphia, PA 19104 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2002年 / 99卷 / 19期
关键词：
protein folding; unfolding rollover; alkaline transition;
D O I：
10.1073/pnas.152439199
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：
Native-state hydrogen exchange experiments under EX1 conditions can distinguish partially unfolded intermediates by their formation rates and identify the amide hydrogens exposed and protected in each. Results obtained define a cytochrome c intermediate seen only poorly before and place it early on the major unfolding pathway. Four distinct unfolding steps are found to be kinetically ordered in the same pathway sequence inferred before.
引用
收藏
页码：12173 / 12178
页数：6
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