Theoretical Conformational Analysis of Disulfide-Linked Tetrapeptides Ac-Cys-Pro-Xaa-Cys-NHMe Having Hydrophobic Xaa Amino-Acid Residues.

DOI DOI Web Site 1 Citations 64 References Open Access
  • Ishikawa Yuichirou
    Department of Applied Chemistry, Osaka Institute of Technology
  • Hirano Yoshiaki
    Department of Applied Chemistry, Osaka Institute of Technology
  • Yoshimoto Jun
    Graduate School of Human Informatics, Nagoya University
  • Oka Masahito
    Research Institute for Advanced Science and Technology, Osaka Prefecture University
  • Hayashi Toshio
    Research Institute for Advanced Science and Technology, Osaka Prefecture University

Bibliographic Information

Other Title
  • Theoretical Conformational Analysis of

Search this article

Description

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.

Journal

  • Polymer Journal

    Polymer Journal 30 (3), 256-261, 1998

    The Society of Polymer Science, Japan

Citations (1)*help

See more

References(64)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top