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

页码：14273 / 14277

页数：5

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