Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H-NMR and photo-CIDNP-NMR spectroscopy

K. H. Mayo, A. Schussheim, G. W. Vuister, R. Boelens, R. Kaptein, M. Engelhard, B. Hess

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Proton-NMR studies of native bacteriorhodopsin revealed the existence of about nine relatively mobile aromatic residues out of the 32 totally present in the protein. These nine comprise approximately three tyrosines, two tryptophans and four phenylalanines. Photo-CIDNP data strongly suggest that, aside from phenylalanines, only one tyrosine and one tryptophan residue are exposed to the solvent. These data are discussed in terms of the current structural model for bacteriorhodopsin.

Original languageEnglish (US)
Pages (from-to)163-168
Number of pages6
JournalFEBS Letters
Volume235
Issue number1-2
DOIs
StatePublished - Aug 1 1988

Keywords

  • Bacteriorhodopsin
  • Membrane protein
  • NMR
  • Photo-CIDNP
  • Proton nuclear resonance
  • Side-chain mobility

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