title: Conformational changes involved in MscL channel gating measured using FRET spectroscopy.
abstract: 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 A upon channel activation.
authors.affiliation: School of Biomedical, Biomolecular and Chemical Science, The University of Western Australia, Crawley, Australia. ben@theochem.uwa.edu.au
authors.forename: Ben
authors.initials: B
authors.lastname: Corry
authors.forename: Paul
authors.initials: P
authors.lastname: Rigby
authors.forename: Zhen-Wei
authors.initials: ZW
authors.lastname: Liu
authors.forename: Boris
authors.initials: B
authors.lastname: Martinac
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry* / Q000648:ultrastructure*; D008081:Liposomes / Q000737:chemistry*; D040542:Mechanotransduction, Cellular; D011487:Protein Conformation
chemical_list: D029968:Escherichia coli Proteins; D007473:Ion Channels; D008081:Liposomes; C086596:MscL protein, E coli