Conformational changes involved in MscL channel gating measured using FRET spectroscopy

被引:54
作者
Corry, B [1 ]
Rigby, P
Liu, ZW
Martinac, B
机构
[1] Univ Western Australia, Sch Biomed Biomol & Chem Sci, Crawley, WA, Australia
[2] Univ Western Australia, Biomed Imaging & Anal Facil, Crawley, WA, Australia
[3] Univ Western Australia, Sch Med & Pharmacol, Crawley, WA, Australia
基金
英国医学研究理事会; 澳大利亚研究理事会;
关键词
D O I
10.1529/biophysj.105.072009
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
We demonstrate that fluorescence resonance energy transfer spectroscopy is a powerful tool for in situ structural analysis of multimeric membrane proteins by measuring the conformational changes involved in gating the mechanosensitive ion channel of large conductance. Ensemble analysis is used to analyze the intensity of light emitted by AlexaFluor-labeled cysteine mutants reconstituted into artificial liposomes before and after acceptor photobleaching. The diameter of the protein is found to increase by 16 angstrom upon channel activation.
引用
收藏
页码:L49 / L51
页数:3
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