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.
引用
收藏
页码:3694 / 3697
页数:4
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