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Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin

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dc.contributor.advisor Ladizhansky, Vladimir
dc.contributor.advisor Brown, Leonid
dc.contributor.author Ward, Meaghan
dc.date.accessioned 2011-09-12T15:34:08Z
dc.date.available 2011-09-12T15:34:08Z
dc.date.copyright 2011-08
dc.date.created 2011-08-22
dc.date.issued 2011-09-12
dc.identifier.uri http://hdl.handle.net/10214/2970
dc.description.abstract High–resolution multidimensional proton-detected NMR was used to study the solvent-exposed regions of a seven-helical integral membrane proton pump proteorhodopsin (PR). Fully deuterated PR samples with protons reintroduced to solvent-accessible sites through back exchange were prepared and found to produce NMR spectra with acceptable proton resolution (~0.2 ppm). Novel three-dimensional proton-detected chemical shift correlation spectroscopy was used for the identification and resonance assignment of the solvent–exposed regions of PR. Though most of the observed residues were located at the membrane interface there were notable exceptions, particularly in helix G. This helix contains the Schiff base-forming Lys231 and many conserved polar residues in the extracellular half. Solvent accessibility of helix G supports the hypothesis that high mobility of the F-G loop could transiently expose a hydrophilic cavity in the extracellular half of PR, and implies that such a cavity may be part of the protein’s proton-conduction pathway. en_US
dc.description.sponsorship Natural Sciences and Engineering Research Council, Ontario Ministry of Training, Colleges, and Universities, Canadian Foundation for Innovation, Ontario Ministry of Research and Innovation, University of Guelph en_US
dc.language.iso en en_US
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/2.5/ca/ *
dc.subject Proteorhodopsin en_US
dc.subject solid-state NMR en_US
dc.subject magic angle spinning en_US
dc.subject Double Quantum Coherence en_US
dc.subject membrane proteins en_US
dc.subject protein-water interaction en_US
dc.title Solid-State NMR Studies of Solvent-Accessible Fragments of a Seven-Helical Transmembrane Protein Proteorhodopsin en_US
dc.type Thesis en_US
dc.degree.programme Biophysics en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Physics en_US
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