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- W2035782169 abstract "Copolypeptides containing the phenylalanine residue were synthesized by the copolymerization of N-carboxy-α-amino acid anhydrides in aprotic solvents. The influence of conformation and configuration, especially of the phenyl pendant group, on the solubility of the copolypeptide in the aprotic solvents was discussed. The copolypeptide of β-benzyl L-aspartate, ε-carbobenzoxy L-lysine, and L-phenylalanine in a ratio 1:1:1 was more soluble in dichloroethan with less helix content than those of copolypeptide of β-benzyl L-aspartate, ε-carbobenzoxy L-lysine, and alanine in a corresponding ratio, or copolypeptides of β-benzyl L-aspartate with ε-carbobenzoxy L-lysine in a ratio 1:1. The insolubility of copolypeptides of L-alanine, L-α-amino n-butyric acid, or L-n-leucine with L-phenylalanine in a ratio of 1:1 was similar to those of poly-L-alanine, -L-α-amino-n-butyric acid, or -L-n-leucine. The dependence of the helix content of these copolypeptides on the phenylalanine residue was complicated. The permeability of water vapor of the copolypeptide films was not affected by the pendant group of the phenyl residue of copolypeptides." @default.
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- W2035782169 date "1988-07-01" @default.
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- W2035782169 title "Solubility and Conformation of High Molecular Weight Synthetic Copolypeptides in Aprotic Solvents. Dependence of the Phenyl Pendant Group on the Solubility and Conformation" @default.
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- W2035782169 doi "https://doi.org/10.1295/polymj.20.557" @default.
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