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• W2050508728 startingPage "1270" @default.
• W2050508728 abstract "The structure and the photocycle of bacteriorhodopsin (bR) containing 13-cis,15-syn retinal, so-called bR548, has been studied by means of molecular dynamics simulations performed on the complete protein. The simulated structure of bR548 was obtained through isomerization of in situ retinal around both its C13-C14 and its C15-N bond starting from the simulated structure of bR568 described previously, containing all-trans,15-anti retinal. After a 50-ps equilibration, the resulting structure of bR548 was examined by replacing retinal by analogues with modified beta-ionone rings and comparing with respective observations. The photocycle of bR548 was simulated by inducing a rapid 13-cis,15-anti-->all-trans,15-syn isomerization through a 1-ps application of a potential that destabilizes the 13-cis isomer. The simulation resulted in structures consistent with the J, K, and L intermediates observed in the photocycle of bR548. The results offer an explanation of why an unprotonated retinal Schiff base intermediate, i.e., an M state, is not formed in the bR548 photocycle. The Schiff base nitrogen after photoisomerization of bR548 points to the intracellular rather than to the extracellular site. The simulations suggest also that leakage from the bR548 to the bR568 cycle arises due to an initial 13-cis,15-anti-->all-trans,15-anti photoisomerization." @default.
• W2050508728 created "2016-06-24" @default.
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• W2050508728 date "1995-04-01" @default.
• W2050508728 modified "2023-09-24" @default.
• W2050508728 title "Molecular dynamics study of the 13-cis form (bR548) of bacteriorhodopsin and its photocycle" @default.
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• W2050508728 doi "https://doi.org/10.1016/s0006-3495(95)80301-2" @default.
• W2050508728 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1282023" @default.
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