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The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy

Abstract:
Making complements: Solid-state MAS NMR spectra of bacteriorhodopsin in its native purple membrane environment can be used to complement crystallographic studies of the protein by validating and redefining the (possibly distorted) loop structures. Backbone dihedral angles were extracted from the chemical shifts and compared to the crystal structures. Where there are conformational differences, the dihedral angles were used to recalculate the loop structure (see picture). © 2011 Wiley-VCH Verlag GmbH and Co. KGaA, Weinheim.

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Publisher copy:
10.1002/anie.201100730

Authors


Higman, VA More by this author
Aslimovska, L More by this author
Sperling, LJ More by this author
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Journal:
Angewandte Chemie - International Edition
Volume:
50
Issue:
36
Pages:
8432-8435
Publication date:
2011-08-29
DOI:
EISSN:
1521-3773
ISSN:
1433-7851
URN:
uuid:9babaa85-17ab-450c-98c8-611c9b635072
Source identifiers:
179565
Local pid:
pubs:179565

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