Conformational Memory of a Protein Revealed by Single-Molecule Spectroscopy

被引:16
|
作者
Schoerner, Mario [1 ,2 ]
Beyer, Sebastian Reinhardt [1 ,2 ]
Southall, June [3 ]
Cogdell, Richard J. [3 ]
Koehler, Juergen [1 ,2 ]
机构
[1] Univ Bayreuth, Expt Phys 5, D-95440 Bayreuth, Germany
[2] Univ Bayreuth, BIMF, D-95440 Bayreuth, Germany
[3] Univ Glasgow, Coll Med Vet & Life Sci, Inst Mol Cell & Syst Biol, Glasgow G12 8QQ, Lanark, Scotland
来源
JOURNAL OF PHYSICAL CHEMISTRY B | 2015年 / 119卷 / 44期
基金
英国生物技术与生命科学研究理事会;
关键词
LIGHT-HARVESTING COMPLEX; FLUORESCENCE INTERMITTENCY; ENERGY LANDSCAPE; RHODOPSEUDOMONAS-ACIDOPHILA; LOW-TEMPERATURE; DYNAMICS; LH2; MOTIONS; ENVIRONMENT; MEMBRANES;
D O I
10.1021/acs.jpcb.5b07494
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Proteins are supramolecular machines that carry out a wide range of different functions, many of which require flexibility. Up until now spontaneous conformational fluctuations of proteins have always been assumed to reflect a stochastic random process. However, if changing between different conformational states was random, then it would be difficult to understand how conformational control of protein function could have evolved. Here we demonstrate that a single protein can show conformational memory. This is exactly the process that can facilitate the evolution of control of switching between two conformational states that can then be used to regulate protein function.
引用
收藏
页码:13964 / 13970
页数:7
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