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pubmed-article:10822532pubmed:abstractText[formula: see text] The conformation of the retinal chromophore in rhodopsin is central for understanding the visual transduction process. The absolute twist around the 12-s bond of the chromophore in rhodopsin has been determined by studies with 11-cis-locked 11,12-cyclopropylretinal analogues (11S,12R)-2 and (11R,12S)-3, enantioselectively synthesized with the aid of an enzyme. The finding that enantiomer 2 binds to opsin while the other 3 does not defines the absolute sense of twist around the 12-s bond.lld:pubmed
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pubmed-article:10822532pubmed:articleTitleEnantioselective binding of an 11-cis-locked cyclopropyl retinal. The conformation of retinal in bovine rhodopsin.lld:pubmed
pubmed-article:10822532pubmed:affiliationDepartment of Chemistry, Columbia University, New York, New York 10027, USA.lld:pubmed
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pubmed-article:10822532pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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