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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Description/Abstract

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.

Item Type: Article
Related URLs:
Divisions: Faculty of Physical and Applied Science > Electronics and Computer Science > NANO
Item ID: 264685
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)
Date: December 2004
Status: Published
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/264685

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