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

doi:10.1016/0014-5793(90)80080-3

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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-muta...

Topics

Animals
Aspartic Acid
Cattle
Energy Transfer
GTP-Binding Proteins
Glutamates
Mutation
Protein Engineering
Recombinant Proteins
Retinal Pigments
Rhodopsin
Schiff Bases
Second Messenger Systems
Spectrophotometry

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