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Biophys. J. BioFAST: First Published September 30, 2005. doi:10.1529/biophysj.105.072009
© 2005 by the Biophysical Society.

A more recent version of this article appeared on December 1, 2005.
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BIOPHYSICAL LETTERS

Conformational Changes Involved in MscL Channel Gating Measured using FRET Spectroscopy

Ben Corry 1*, Paul Rigby 1, Zhen-Wei Liu 1 and Boris Martinac 1

1 University of Western Australia

* To whom correspondence should be addressed. E-mail: ben{at}theochem.uwa.edu.au.

Submitted on August 4, 2005
Revised on August 18, 2005
Accepted on 13 September 2005


  Abstract
We demonstrate that FRET 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 MscL. 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 16Å upon channel activation.

Key Words: FRET, Gating, Ion channel, Mechanosensitive channel, MscL, Structural biology




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Copyright © 2005 by the Biophysical Society.