Biochemistry - How soft is a protein? A protein dynamics force constant measured by neutron scattering

被引:654
作者
Zaccai, G
机构
[1] Inst Biol Struct, F-38027 Grenoble 1, France
[2] Inst Max Von Laue Paul Langevin, F-38042 Grenoble 9, France
关键词
D O I
10.1126/science.288.5471.1604
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
An effective environmental force constant is introduced to quantify the molecular resilience (or its opposite, "softness") of a protein structure and relate it to biological function and activity. Specific resilience-function relations were found in neutron-scattering experiments on purple membranes containing bacteriorhodopsin, the light-activated proton pump of halobacteria; the connection between resilience and stability is illustrated by a study of myoglobin in different environments. Important advantages of the neutron method are that it can characterize the dynamics of any type of biological sample-which need not be crystalline or monodisperse-and that it enables researchers to focus on the dynamics of specific parts of a complex structure with deuterium labeling.
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页码:1604 / 1607
页数:4
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