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Theoretical conformational analysis of tetrapeptide Ac-Cys-Pro-Gly-Cys-NHMe with disulfide linkage

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Summary

Theoretical conformational analysis was carried out for the acyclic and cyclic tetrapeptides Ac-Cys-Pro-Gly-Cys-NHMe using ECEPP and optimization procedure for investigating the conformational preference of peptides having disulfide linkage. Calculated results indicate that cyclic Ac-Cys-Pro-Gly-Cys-NHMe forms compactly fold conformations wity type II β-bend at the Pro-Gly portion, and also show fairly good agreement with experimental results of the NMR spectroscopy for the tetrapeptides having Cys-Pro-Gly-Cys sequence.

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Authors and Affiliations

  1. Graduate School of Human Informatics, Nagoya University, Chikusa-ku, 464-01, Nagoya, Japan

    Jun Yoshimoto

  2. Department of Applied Chemistry, Osaka Institute of Technology, Asahi-ku, 535, Osaka, Japan

    Akira Nishinaga

  3. Research Institute of Advanced Science and Technology, Osaka Prefecture University, 593, Sakai, Osaka, Japan

    Masahito Oka & Toshio Hayashi

Authors
  1. Jun Yoshimoto
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  2. Akira Nishinaga
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  3. Masahito Oka
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  4. Toshio Hayashi
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Yoshimoto, J., Nishinaga, A., Oka, M. et al. Theoretical conformational analysis of tetrapeptide Ac-Cys-Pro-Gly-Cys-NHMe with disulfide linkage. Polymer Bulletin 38, 109–115 (1997). https://doi.org/10.1007/s002890050026

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  • DOI: https://doi.org/10.1007/s002890050026

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