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

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, as...

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Published inFEBS letters Vol. 235; no. 1-2; pp. 163 - 168
Main Authors Mayo, K.H., Schussheim, A., Vuister, G.W., Boelens, R., Kaptein, R., Engelhard, M., Hess, B.
Format Journal Article
LanguageEnglish
Published 01.08.1988
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)81255-9