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Article

Asp83, Glu113 and Glu134 are not specifically involved in Schiff base protonation or wavelength regulation in bovine rhodopsin.

FEBS letters - 15 Jan 1990

Janssen J J, De Caluwé G L, De Grip W J

Abstract excerpt

Site-specific mutagenesis was employed to investigate the proposed contribution of proton-donating residues (Glu, Asp) in the membrane domains of bovine rhodopsin to protonation of the Schiff base-linking protein and chromophore or to wavelength modulation of this visual pigment. Three point-mutations were introduced to replace the highly conserved residues Asp83 by Asn (D83N), Glu113 by Gln (E113 Q) or Glu134 by...

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Identifiers

PMID: 2105232
DOI: 10.1016/0014-5793(90)80080-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Asp83, Glu113 and Glu134 are not specifically involved in Schiff base protonation or wavelength regulation in bovine rhodopsin.PMID 2105232Read ↗

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