Abstract
To investigate the short-range interactions in gramicidin A, conformational energy calculations using an Empirical Conformational Energy Program for Peptides (ECEPP) were carried out on N-acetyl-N′-methylamide of L-Ala–D-Ala dipeptide. The conformational energy was minimized from the starting conformations which included all combinations of low-energy single-residue minima. It was found that the calculated bend probability of the L–Ala–D-Ala sequence is significantly higher than that of the L-Ala–L-Ala sequence, and that type II β-bend is the most favorable conformation.
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Oka, M., Nakajima, A. Theoretical Conformational Analysis on N-Acetyl-N′-methylamide of L-Ala-D-Ala Dipeptide. Polym J 16, 553–558 (1984). https://doi.org/10.1295/polymj.16.553
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DOI: https://doi.org/10.1295/polymj.16.553