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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1990-6-12
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pubmed:abstractText |
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 recent proposal that the observed biphasic CD spectrum of bR is due to the superposition of the CD spectra having opposite signs of more than one type of bR rather than due to exciton coupling.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
26
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
155-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2185945-Bacteriorhodopsins,
pubmed-meshheading:2185945-Binding Sites,
pubmed-meshheading:2185945-Circular Dichroism,
pubmed-meshheading:2185945-DNA, Recombinant,
pubmed-meshheading:2185945-Escherichia coli,
pubmed-meshheading:2185945-Halobacterium,
pubmed-meshheading:2185945-Mutation,
pubmed-meshheading:2185945-Protein Conformation,
pubmed-meshheading:2185945-Tyrosine
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pubmed:year |
1990
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pubmed:articleTitle |
Sensitivity of the retinal circular dichroism of bacteriorhodopsin to the mutagenetic single substitution of amino acids: tyrosine.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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