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• W1970034345 abstract "Trans-cis isomerization of a proline peptide bond is a potential mechanism to open the channel of the 5-HT(3) receptor. Here, we have used the metadynamics method to theoretically explore such a mechanism. We have determined the free energy surfaces in aqueous solution of a series of dipeptides of proline analogues and evaluated the free energy difference between the cis and trans isomers. These theoretical results were then compared with data from mutagenesis experiments, in which the response of the 5-HT(3) receptor was measured when the proline at the apex of the M2-M3 transmembrane domain loop was mutated. The strong correlation between the experimental and the theoretical data supports the existence of a trans-cis proline switch for opening the 5-HT(3) receptor ion channel." @default.
• W1970034345 created "2016-06-24" @default.
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• W1970034345 date "2009-08-10" @default.
• W1970034345 modified "2023-10-14" @default.
• W1970034345 title "Trans−cis Switching Mechanisms in Proline Analogues and Their Relevance for the Gating of the 5-HT₃ Receptor" @default.
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• W1970034345 doi "https://doi.org/10.1021/jp9046962" @default.
• W1970034345 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2733763" @default.
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• W1970034345 hasPublicationYear "2009" @default.
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