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Compositional And Environmental Dependence Of The Stability Of Α-Helices

Author

Listed:
  • CHANGJUN CHEN

    (Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China)

  • JIANHUI FENG

    (Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China)

  • LINSEN ZHANG

    (Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China)

  • YI XIAO

    (Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China)

Abstract

The stability of α-helices in proteins depends on both their compositions and environments. To see how these two factors match with each other, we selected three typical α-helices from real proteins each of them has different compositions of hydrophobic and hydrophilic amino acids. We simulated the dynamics of the three helices in vacuum and in water using molecular dynamics. The results show that the stabilities of the three α-helices are different in vacuum and in water, which are consistent with their locations in the proteins. We also found some interesting behaviors of these α-helices.

Suggested Citation

  • Changjun Chen & Jianhui Feng & Linsen Zhang & Yi Xiao, 2005. "Compositional And Environmental Dependence Of The Stability Of Α-Helices," International Journal of Modern Physics C (IJMPC), World Scientific Publishing Co. Pte. Ltd., vol. 16(10), pages 1597-1608.
    • Handle: RePEc:wsi:ijmpcx:v:16:y:2005:i:10:n:s0129183105008187
    DOI: 10.1142/S0129183105008187
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