Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H-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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Bibliographic Details
Published inFEBS letters Vol. 235; no. 1; 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 Elsevier B.V 01.08.1988
Subjects
Bacteriorhodopsin
bR, bacteriorhodopsin
CIDNP, chemically induced dynamic nuclear polarization
FID, free induction decay
Membrane protein
NMR
Photo-CIDNP
Proton nuclear resonance
Side-chain mobility
TSP, trimethylsilyl-1-propanesulfonate
Bacteriorhodopsin
Membrane protein
Proton nuclear resonance
NMR
Photo-CIDNP
CIDNP, chemically induced dynamic nuclear polarization
bR, bacteriorhodopsin
TSP, trimethylsilyl-1-propanesulfonate
FID, free induction decay
Side-chain mobility
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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