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 journalArticlepeer-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 languageEnglish (US)
Pages (from-to)8432-8435
Number of pages4
JournalAngewandte Chemie - International Edition
Volume50
Issue number36
DOIs
StatePublished - Aug 29 2011

Keywords

  • NMR spectroscopy
  • bacteriorhodopsin
  • membrane proteins
  • protein structures

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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