Resonance Raman study of the dark-adapted form of the purple membrane protein

B. Aton, A. G. Doukas, Robert Callender, B. Becher, T. G. Ebrey

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The resonance Raman spectrum of the dark-adapted form of the purple membrane protein (bacteriorhodopsin) has been obtained and is compared to the light-adapted pigment and model chromophore spectra. As in the light-adapted form, the chromophore-protein linkage is found to be a protonated Schiff base. Electron delocalization appears to play the dominant role in color regulation. The dark-adapted spectrum indicates a conformation closer to 13-cis than the light-adapted spectrum.

Original languageEnglish (US)
Pages (from-to)424-428
Number of pages5
JournalBBA - Protein Structure
Volume576
Issue number2
DOIs
StatePublished - Feb 26 1979
Externally publishedYes

Fingerprint

Purple Membrane
Membrane Proteins
Chromophores
Light
Bacteriorhodopsins
Schiff Bases
Pigments
Conformations
Raman scattering
Color
Electrons
Proteins

Keywords

  • (Purple membrane)
  • Bacteriorhodopsin
  • Chromaphore-protein linkage
  • Dark-adapted spectrum
  • Raman resonance

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Resonance Raman study of the dark-adapted form of the purple membrane protein. / Aton, B.; Doukas, A. G.; Callender, Robert; Becher, B.; Ebrey, T. G.

In: BBA - Protein Structure, Vol. 576, No. 2, 26.02.1979, p. 424-428.

Research output: Contribution to journalArticle

Aton, B. ; Doukas, A. G. ; Callender, Robert ; Becher, B. ; Ebrey, T. G. / Resonance Raman study of the dark-adapted form of the purple membrane protein. In: BBA - Protein Structure. 1979 ; Vol. 576, No. 2. pp. 424-428.
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AU - Ebrey, T. G.

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