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- W2103986230 endingPage "2290" @default.
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- W2103986230 abstract "To our knowledge, we present the first constant-pH molecular dynamics study of the neuropeptide kyotorphin in the presence of an explicit lipid bilayer. The overall conformation freedom of the peptide was found to be affected by the interaction with the membrane, in accordance with previous results using different methodologies. Analysis of the interactions between the N-terminus amine group of the peptide and several lipid atoms shows that the membrane is able to stabilize both ionized and neutral forms of kyotorphin, resulting in a pKa value that is similar to the one obtained in water. This illustrates how a detailed molecular model of the membrane leads to rather different results than would be expected from simply regarding it as a low-dielectric slab." @default.
- W2103986230 created "2016-06-24" @default.
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- W2103986230 date "2015-05-01" @default.
- W2103986230 modified "2023-09-28" @default.
- W2103986230 title "Constant-pH Molecular Dynamics Study of Kyotorphin in an Explicit Bilayer" @default.
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- W2103986230 doi "https://doi.org/10.1016/j.bpj.2015.03.052" @default.
- W2103986230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4423061" @default.
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