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- W3132692495 abstract "The interaction of peptides with membrane lipids is significant in the biological processes. Short peptides are an excellent alternative to the immune response antibodies, and they play a very crucial role in binding, insertion, and folding of membrane proteins. The characterization of solvent-dependent conformational ensemble of the peptides is required for a molecular-level understanding of the thermodynamic hydrophobicity scale. To characterize the solvent-peptide interactions, we have developed a computational procedure that allows us to accurately model the peptides in both aqueous and organic solvent conditions and determine their properties at a thermodynamic level." @default.
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- W3132692495 date "2021-02-01" @default.
- W3132692495 modified "2023-10-17" @default.
- W3132692495 title "Developing Efficient Transfer Free Energy Calculation Methods for Hydrophobicity Predictions" @default.
- W3132692495 doi "https://doi.org/10.1016/j.bpj.2020.11.913" @default.
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