Lattice model of transmembrane polypeptide folding

C. M. Chen*

*此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

15 引文 斯高帕斯(Scopus)

摘要

Folding of hydrophobic polypeptides into unique three-dimensional structures in a membrane is investigated by Monte Carlo simulations using the bond fluctuation model. Its ground stale structure can be a helix or a double helix depending on the competition of hydrogen bonding and backbone bending energies. The folding pathway of hydrophobic polypeptides in a nonpolar environment is found to favor the helical structure over the double helix. The folding time of a transmembrane domain increases exponentially with the chain length. Folding at low temperatures exhibits an Arrhenius-like behavior. We discuss the kinetics of both random folding and channel complex assisted folding of a polypeptide chain. Our results suggest a significantly smaller energetic barrier in the folding pathway for channel complex assisted folding.

原文英語
文章編號010901
頁(從 - 到)109011-109014
頁數4
期刊Physical Review E - Statistical, Nonlinear, and Soft Matter Physics
63
發行號1 I
DOIs
出版狀態已發佈 - 2001

ASJC Scopus subject areas

  • 統計與非線性物理學
  • 統計與概率
  • 凝聚態物理學

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