Folding of a three-helix bundle at the folding speed limit

被引：52

作者：

Wang, T ^{[1
]}

Zhu, YJ ^{[1
]}

Gai, F ^{[1
]}

机构：

[1] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2004年 / 108卷 / 12期

关键词：

D O I：

10.1021/jp049652q

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We show in this Letter that a double mutant (K51/K39V) of 1prb(7-53), the GA module of an albumin binding domain, has a maximum folding rate constant of similar to1 (mus)(-1). This value is comparable to the estimated theoretical speed limit for protein folding. In addition, we found that the mean hydrophobicity of a given tertiary fold plays an important role in controlling its folding rate.

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页码：3694 / 3697

页数：4

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