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Article

Sensitivity of the retinal circular dichroism of bacteriorhodopsin to the mutagenetic single substitution of amino acids: tyrosine.

FEBS letters - 26 Mar 1990

Du J J, el-Sayed M A, Stern L J, Mogi T, Khorana H G

Abstract excerpt

Bacteriorhodopsin (bR) in the native purple membrane, in wild type expressed in E. coli and reconstituted in lipid vesicles, and its constituted mutants with substitutions of Tyr-185 by Phe all are found to have different visible retinal CD spectra. The results strongly suggest that the environment of the retinal in bR determines the sign and heterogeneity of its visible retinal CD spectrum. This supports the...

Topics

Bacteriorhodopsins
Binding Sites
Circular Dichroism
DNA, Recombinant
Escherichia coli
Halobacterium
Mutation
Protein Conformation
Tyrosine

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2185945
DOI: 10.1016/0014-5793(90)80178-l

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2185945-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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