The Conformation of Bacteriorhodopsin Loops in Purple Membranes Resolved by Solid-State MAS NMR Spectroscopy

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 che...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2011-08, Vol.50 (36), p.8432-8435
Main Authors: Higman, Victoria A., Varga, Krisztina, Aslimovska, Lubica, Judge, Peter J., Sperling, Lindsay J., Rienstra, Chad M., Watts, Anthony
Format: Article
Language:English
Subjects:
bacteriorhodopsin
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - metabolism
Crystallography, X-Ray
membrane proteins
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Tertiary
protein structures
Purple Membrane - metabolism
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Summary: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).
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201100730