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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2010-6-30
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pubmed:abstractText |
The presence of a biphasic circular dichroism (CD) observed in the visible absorption spectrum of retinal in bacteriorhodopsin (bR) has been believed for many years to be due to excitonic-type interaction within the trimeric structure of the retinal in the protein membrane. In the present work, we present data and discuss previous observations that strongly suggest the absence of such an excitonic interaction. The magnetic CD spectrum of the trimer is found to be similar to that of the monomer and shows no sign of absorption to the doubly degenerate state predicted to be present from the exciton theory. This, together with the previous observations on the CD spectra of the photocycle intermediates of bR as well as the linear polarization studies of the fluorescence and the daughter absorption, sheds doubt on the presence of exciton interaction and thus suggests the presence of neither an antenna system nor a viable special reaction center in bR. Possible explanation for the observed biphasic nature of the CD spectrum is given in terms of having more than one type of bR with different protein conformations around the retinals in the trimer giving each similar absorption maximum but opposite signs for its rotary dispersion power.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-10022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-1152049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-1161000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-1201079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-1247534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-1259746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-16593973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-16598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-19431693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-239244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-3363359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-4699992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-4940442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-6278477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-6287921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-6594682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-6941281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-7074194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-875024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16594053-963229
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pubmed:language |
eng
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pubmed:journal |
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pubmed:status |
PubMed-not-MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5376-9
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pubmed:dateRevised |
2010-9-15
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pubmed:year |
1989
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pubmed:articleTitle |
Is there an excitonic interaction or antenna system in bacteriorhodopsin?
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90024.
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pubmed:publicationType |
Journal Article
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