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利用单分子光谱法连接构象动力学与功能

Bridging conformational dynamics and function using single-molecule spectroscopy.

作者信息

Myong Sua, Stevens Benjamin C, Ha Taekjip

机构信息

Department of Physics, University of Illinois, Urbana-Champaign, Urbana, Illinois 61801, USA.

出版信息

Structure. 2006 Apr;14(4):633-43. doi: 10.1016/j.str.2006.02.005.

DOI:10.1016/j.str.2006.02.005
PMID:16615904
Abstract

In a typical structure-function relation study, the primary structure of proteins or nucleic acids is changed by mutagenesis and its functional effect is measured via biochemical means. Single-molecule spectroscopy has begun to give a whole new meaning to the "structure-function relation" by measuring the real-time conformational changes of individual biological macromolecules while they are functioning. This review discusses a few recent examples: untangling internal chemistry and conformational dynamics of a ribozyme, branch migration landscape of a Holliday junction at a single-step resolution, tRNA selection and dynamics in a ribosome, repetitive shuttling and snapback of a helicase, and discrete rotation of an ATP synthase.

摘要

在典型的结构-功能关系研究中,蛋白质或核酸的一级结构通过诱变改变,其功能效应通过生化手段测定。单分子光谱通过测量单个生物大分子在发挥功能时的实时构象变化,开始赋予“结构-功能关系”全新的意义。本综述讨论了一些近期的例子:解开核酶的内部化学和构象动力学、以单步分辨率观察霍利迪连接体的分支迁移图谱、核糖体中的tRNA选择和动力学、解旋酶的重复穿梭和回折,以及ATP合酶的离散旋转。

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Bridging conformational dynamics and function using single-molecule spectroscopy.利用单分子光谱法连接构象动力学与功能
Structure. 2006 Apr;14(4):633-43. doi: 10.1016/j.str.2006.02.005.
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Spotlighting motors and controls of single FoF1-ATP synthase.聚焦于单体 FoF1-ATP 合酶的马达和控制。
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