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Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy.

Abstract:

We report for the first time, oriented-sample solid-state NMR experiments, specifically polarization inversion spin exchange at the magic angle (PISEMA) and 1H-15N heteronuclear chemical shift correlation (HETCOR), applied to an integral seven-transmembrane protein, bacteriorhodopsin (bR), in natural membranes. The spectra of [15N]Met-bR revealed clearly distinguishable signals from the helical and loop regions. By deconvolution of the helix resonances, it was possible to establish constraint...

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Publication status:
Published

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Publisher copy:
10.1016/j.jsb.2004.10.002

Authors


Journal:
Journal of structural biology
Volume:
149
Issue:
1
Pages:
7-16
Publication date:
2005-01-01
DOI:
EISSN:
1095-8657
ISSN:
1047-8477
Source identifiers:
100059
Language:
English
Keywords:
Pubs id:
pubs:100059
UUID:
uuid:c293e050-cc2b-469a-b1f1-df0a2c439b50
Local pid:
pubs:100059
Deposit date:
2012-12-19

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