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Alpha-Helix Formation In C-Peptide Rnase-A Investigated By Parallel Tempering Simulations

Author

Listed:
  • GÖKHAN GÖKOĞLU

    (Department of Physics Engineering, Hacettepe University, 06800 Beytepe, Ankara, Turkey)

  • TARIK ÇELİK

    (Turkish Academy of Sciences, Piyade Sokak No. 27, 06550 Çankaya, Ankara, Turkey)

Abstract

We have performed parallel tempering simulations of a 13-residue peptide fragment of ribonuclease-A, c-peptide, in implicit solvent with constant dielectric permittivity. This peptide has a strong tendency to form α-helical conformations in solvent as suggested by circular dichroism (CD) and nuclear magnetic resonance (NMR) experiments. Our results demonstrate that 5th and 8–12 residues are in the α-helical region of the Ramachandran map for global minimum energy state in solvent environment. Effects of salt bridge formation on stability of α-helix structure are discussed.

Suggested Citation

  • Gökhan Gökoğlu & Tarik Çeli̇k, 2007. "Alpha-Helix Formation In C-Peptide Rnase-A Investigated By Parallel Tempering Simulations," International Journal of Modern Physics C (IJMPC), World Scientific Publishing Co. Pte. Ltd., vol. 18(01), pages 91-98.
    • Handle: RePEc:wsi:ijmpcx:v:18:y:2007:i:01:n:s0129183107010292
    DOI: 10.1142/S0129183107010292
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