Direct observation of correlated interdomain motion in alcohol dehydrogenase

被引：65

作者：

Biehl, Ralf ^{[1
]}

Hoffmann, Bernd ^{[2
]}

Monkenbusch, Michael ^{[1
]}

Falus, Peter ^{[3
]}

Preost, Sylvain ^{[4
]}

Merkel, Rudolf ^{[2
]}

Richter, Dieter ^{[1
]}

机构：

[1] Forschungszentrum Julich, Inst Festkorperforsch, D-52425 Julich, Germany

[2] Forschungszentrum Julich, Inst Bio & Nanosyst, D-52425 Julich, Germany

[3] Inst Max Von Laue Paul Langevin, F-38042 Grenoble, France

[4] Hahn Meitner Inst Berlin GmbH, D-14109 Berlin, Germany

来源：

PHYSICAL REVIEW LETTERS | 2008年 / 101卷 / 13期

关键词：

D O I：

10.1103/PhysRevLett.101.138102

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spinecho spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.

引用

页数：4

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