Abstract
Random-coiled conformations of poly(L-phenylalanine) and poly(L-tyrosine) were theoretically analyzed by a conformational energy calculation based on intra-residue interactions. Favorable side-chain/backbone interactions stabilizing extended conformations were found. Owing to these interactions, the characteristic ratios of poly(L-phenylalanine) and poly(L-tyrosine) were significantly higher than that of poly(L-alanine). The theoretical characteristic ratio of poly(L-tyrosine) was in good agreement with the experimental results for the side-chain derivative of poly(L-tyrosine).
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Oka, M., Nakajima, A. Random-Coiled Conformation of Polypeptide Chains I. Theoretical Conformational Analysis of Polypeptide Chains with Aromatic Side Chains. Polym J 16, 693–709 (1984). https://doi.org/10.1295/polymj.16.693
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DOI: https://doi.org/10.1295/polymj.16.693
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