Solid-State 17O NMR as a Probe for Structural Studies of Proteins in Biomembranes
Lemaître, V, de Planque, MRR, Howes, AP, Smith, ME, Dupree, R and Watts, A (2004) Solid-State 17O NMR as a Probe for Structural Studies of Proteins in Biomembranes. Journal of the American Chemical Society, 126, (47), 15320-15321.
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We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O-[Ala12]-WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply 17O NMR to the study of membrane-incorporated peptides. Furthermore, we were able to estimate distances within the selectively labeled WALP peptide, which represents a consensus transmembrane protein sequence. This work opens up new applications of 17O solid-state NMR on biological systems.
|Divisions:||Faculty of Physical and Applied Science > Electronics and Computer Science > NANO
|Date Deposited:||16 Oct 2007|
|Last Modified:||02 Mar 2012 14:05|
|Contributors:||Lemaître, V (Author)
de Planque, MRR (Author)
Howes, AP (Author)
Smith, ME (Author)
Dupree, R (Author)
Watts, A (Author)
|Further Information:||Google Scholar|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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