Dansylation of bacteriorhodopsin near the retinal attachment site

G. Harris, R. Renthal, J. Tuley, N. Robinson

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

The purple membrane of Halobacterium halobium was reacted with 5-dimethylaminonaphthalene-l-sulfonyl chloride (dansyl chloride) at pH 8.0. Chromophoric and functional properties of the product appear unaltered. Approximately 2 moles of dansyl group were incorporated per mole of bacteriorhodopsin, part bound to bacteriorhodopsin and part bound to lipids. Purification and fragmentation of the protein showed most of the dansyl modification in a fragment containing residues 33 to 56. Amino acid analysis indicates that the major dansylated site is lysine 40. We conclude that, contrary to published models, 1) bacteriorhodopsin folds in a way that exposes lysine 40 at the membrane surface, and 2) this side chain is not involved in the proton pump mechanism.

Original languageEnglish (US)
Pages (from-to)926-931
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume91
Issue number3
DOIs
StatePublished - Dec 14 1979

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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