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

doi:10.1016/0014-5793(88)81255-9

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

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

15 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 language	English (US)
Pages (from-to)	163-168
Number of pages	6
Journal	FEBS Letters
Volume	235
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(88)81255-9
State	Published - Aug 1 1988

Bibliographical note

Funding Information:
AcknowledgementTsh: is work was supported by a grant from the North Atlantic Treaty Organization (NATO) Scientific Affairs Division (RG.85/0424). A.S. received a Summer Research Fellowship from Yale University. We thank J. Piittmann-Wunderlich and A. Scholz for excellent technical help.

Keywords

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

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

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.",

keywords = "Bacteriorhodopsin, Membrane protein, NMR, Photo-CIDNP, Proton nuclear resonance, Side-chain mobility",

author = "Mayo, {K. H.} and A. Schussheim and Vuister, {G. W.} and R. Boelens and R. Kaptein and M. Engelhard and B. Hess",

note = "Funding Information: AcknowledgementTsh: is work was supported by a grant from the North Atlantic Treaty Organization (NATO) Scientific Affairs Division (RG.85/0424). A.S. received a Summer Research Fellowship from Yale University. We thank J. Piittmann-Wunderlich and A. Scholz for excellent technical help.",

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T1 - Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H-NMR and photo-CIDNP-NMR spectroscopy

AU - Mayo, K. H.

AU - Schussheim, A.

AU - Vuister, G. W.

AU - Boelens, R.

AU - Kaptein, R.

AU - Engelhard, M.

AU - Hess, B.

N1 - Funding Information: AcknowledgementTsh: is work was supported by a grant from the North Atlantic Treaty Organization (NATO) Scientific Affairs Division (RG.85/0424). A.S. received a Summer Research Fellowship from Yale University. We thank J. Piittmann-Wunderlich and A. Scholz for excellent technical help.

PY - 1988/8/1

Y1 - 1988/8/1

N2 - 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.

AB - 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.

KW - Bacteriorhodopsin

KW - Membrane protein

KW - NMR

KW - Photo-CIDNP

KW - Proton nuclear resonance

KW - Side-chain mobility

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