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Helix conformations in 7TM membrane proteins determined using oriented-sample solid-state NMR with multiple residue-specific 15N labeling.

Abstract:

Oriented solid-state NMR in combination with multiple-residue-specific (15)N labeling and extensive numerical spectral analysis is proposed to determine helix conformations of large membrane proteins in native membranes. The method is demonstrated on uniaxially oriented samples of (15)N-methionine, -valine, and -glycine-labeled bacteriorhopsin in native purple membranes. Experimental two-dimensional (1)H-(15)N dipole-dipole coupling versus (15)N chemical shift spectra for all samples are anal...

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Publication status:
Published

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Publisher copy:
10.1529/biophysj.107.116004

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Biophysical journal
Volume:
94
Issue:
1
Pages:
241-250
Publication date:
2008-01-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:f7e0d010-c4c4-4698-82b5-4d97b8fb98cc
Source identifiers:
100746
Local pid:
pubs:100746

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