Suppr超能文献

蛋白质有多柔软?通过中子散射测量的蛋白质动力学力常数。

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

作者信息

Zaccai G

机构信息

Institut de Biologie Structurale, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France.

出版信息

Science. 2000 Jun 2;288(5471):1604-7. doi: 10.1126/science.288.5471.1604.

Abstract

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.

摘要

引入一个有效的环境力常数来量化蛋白质结构的分子弹性(或其相反的“柔软性”),并将其与生物学功能和活性联系起来。在对含有细菌视紫红质(嗜盐菌的光激活质子泵)的紫色膜进行的中子散射实验中发现了特定的弹性-功能关系;通过对处于不同环境中的肌红蛋白的研究,阐明了弹性与稳定性之间的联系。中子方法的重要优点在于,它可以表征任何类型生物样品的动力学——这些样品不一定是晶体或单分散的——并且它使研究人员能够通过氘标记专注于复杂结构特定部分的动力学。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验