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

Victoria A. Higman; Krisztina Varga; Lubica Aslimovska; Peter J. Judge; Lindsay J. Sperling; Chad M. Rienstra; Anthony Watts

doi:10.1002/anie.201100730

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

Victoria A. Higman, Krisztina Varga, Lubica Aslimovska, Peter J. Judge, Lindsay J. Sperling, Chad M. Rienstra, Anthony Watts

Research output: Contribution to journal › Article › peer-review

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).

Original language	English (US)
Pages (from-to)	8432-8435
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	36
DOIs	https://doi.org/10.1002/anie.201100730
State	Published - Aug 29 2011

Keywords

NMR spectroscopy
bacteriorhodopsin
membrane proteins
protein structures

ASJC Scopus subject areas

Catalysis
Chemistry(all)

Online availability

10.1002/anie.201100730

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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).",

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AU - Varga, Krisztina

AU - Aslimovska, Lubica

AU - Judge, Peter J.

AU - Sperling, Lindsay J.

AU - Rienstra, Chad M.

AU - Watts, Anthony

PY - 2011/8/29

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AB - 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).

KW - NMR spectroscopy

KW - bacteriorhodopsin

KW - membrane proteins

KW - protein structures

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

Abstract

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