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Originally published as Biophys J. BioFAST on September 30, 2005.
doi:10.1529/biophysj.105.072009
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Biophysical Journal 89:L49-L51 (2005)
© 2005 The Biophysical Society

Conformational Changes Involved in MscL Channel Gating Measured using FRET Spectroscopy

Ben Corry *, Paul Rigby {dagger}, Zhen-Wei Liu {ddagger} and Boris Martinac {ddagger}

* School of Biomedical, Biomolecular and Chemical Science, {dagger} Biomedical Imaging and Analysis Facility, and {ddagger} School of Medicine and Pharmacology, The University of Western Australia, Crawley, Australia

Correspondence: Address reprint requests to Dr. Ben Corry, Tel.: 61-8-6488-3166; E-mail: ben{at}theochem.uwa.edu.au.

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 Å upon channel activation.




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