Abstract
Theoretical conformational analysis was carried out on four cyclic tetrapeptides Ac-Cys-Pro-Xaa-Cys-NHMe (Xaa=Val, Phe, Leu, and norleucine) using Empirical Conformation Energy Program for Peptides (ECEPP) and optimization procedure for investigating the effects of differences in the hydrophonbic side-chain groups of Xaa residue on the β-bend conformation at the Xaa-Pro portion of cyclic peptides having the disulfide linkage. Calculated results indicate that four cyclic Ac-Cys-Pro-Xaa-Cys-NHMe essentially form type III β-bend at the Pro-Xaa portion, and also show fairly good agreement with experimental results of the NMR spectroscopy and X-ray crystallography for the tetrapeptides having Cys-Pro-Xaa-Cys sequence.
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Ishikawa, Y., Hirano, Y., Yoshimoto, J. et al. Theoretical Conformational Analysis of Disulfide-Linked Tetrapeptides Ac-Cys-Pro-Xaa-Cys-NHMe Having Hydrophobic Xaa Amino-Acid Residues. Polym J 30, 256–261 (1998). https://doi.org/10.1295/polymj.30.256
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DOI: https://doi.org/10.1295/polymj.30.256