Coupling of protein relaxation to ligand binding and migration in myoglobin

被引：28

作者：

Agmon, N ^{[1
]}

机构：

[1] Hebrew Univ Jerusalem, Dept Phys Chem, IL-91904 Jerusalem, Israel

来源：

BIOPHYSICAL JOURNAL | 2004年 / 87卷 / 03期

关键词：

D O I：

10.1529/biophysj.104.042929

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Protein relaxation, ligand binding, and ligand migration into a hydrophobic cavity in myoglobin are unified by a bounded diffusion model which produces an accurate fit to complex ligand rebinding data over eight decades in time and a 160 K temperature range, in qualitative agreement with time-resolved x-ray crystallography. Protein relaxation operates in a cyclic manner to move the ligand away from the binding site.

引用

页码：1537 / 1543

页数：7

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