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- W2065005058 abstract "We statistically analyzed the experimentally determined 1-octanol/water partition coefficient, log P, of a wide variety of N-acetyl-di- and tripeptide amides and unblocked di- and tripeptides to evaluate the hydrophobic parameters of the amino acid side chains of peptides. For blocked peptides, hydrophobic parameters were defined for amino acids having un-ionizable and ionizable side chains. For unblocked peptides, hydrophobic parameters were evaluated for 12 amino acids with un-ionizable side chains. In order to estimate the hydrophobic parameters for unnatural and ionizable amino acids, a procedure was developed based on the relationship between our hydrophobic parameters and the log P values of model amino acids calculated by the fragment constant method. Use of the hydrophobic parameters in quantitative structure-activity relationship (QSAR) studies of bioactive peptides and conformational studies of proteins have also been presented." @default.
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- W2065005058 date "1997-03-01" @default.
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- W2065005058 title "Evaluation of the hydrophobic parameters of the amino acid side chains of peptides and their application in QSAR and conformational studies" @default.
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- W2065005058 doi "https://doi.org/10.1016/s0166-1280(97)90371-7" @default.
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