Bridging conformational dynamics and function using single-molecule spectroscopy

被引：47

作者：

Myong, S

Stevens, BC

Ha, T ^{[1
]}

机构：

[1] Univ Illinois, Dept Phys, Urbana, IL 61801 USA

[2] Howard Hughes Med Inst, Urbana, IL 61801 USA

来源：

STRUCTURE | 2006年 / 14卷 / 04期

关键词：

D O I：

10.1016/j.str.2006.02.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 realtime 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.

引用

收藏

页码：633 / 643

页数：11

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