What is the role of non-native intermediates of β-lactoglobulin in protein folding?

被引：42
|
作者：
Chikenji, G [1 ]
Kikuchi, M [1 ]
机构：
[1] Osaka Univ, Grad Sch Sci, Dept Phys, Toyonaka, Osaka 5600043, Japan
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2000年 / 97卷 / 26期
关键词：
D O I：
10.1073/pnas.97.26.14273
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 mechanism of alpha --> beta transition in folding of beta -lactoglobulin is discussed based on free energy landscape analysis of a long lattice model. It is found that helical propensity of beta -lactoglobulin is driven by conformational entropy and is intrinsically coded in its native structure. We propose a view on a role of folding intermediate, which is "on-pathway" but rich in non-native structures. The present results suggest that the native structure topology plays an important role in alpha --> beta transition.
引用
收藏
页码：14273 / 14277
页数：5
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