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The Conformation of Bacteriorhodopsin Loops in Purple Membranes Resolved by Solid‐State MAS NMR Spectroscopy
Author(s) -
Higman Victoria A.,
Varga Krisztina,
Aslimovska Lubica,
Judge Peter J.,
Sperling Lindsay J.,
Rienstra Chad M.,
Watts Anthony
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201100730
Subject(s) - bacteriorhodopsin , dihedral angle , crystallography , solid state , chemistry , complement (music) , nuclear magnetic resonance spectroscopy , solid state nuclear magnetic resonance , crystal structure , spectroscopy , loop (graph theory) , membrane , physics , stereochemistry , nuclear magnetic resonance , molecule , hydrogen bond , mathematics , combinatorics , biochemistry , organic chemistry , quantum mechanics , complementation , gene , phenotype
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).