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 |
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文章編號 | 010901 |
頁(從 - 到) | 109011-109014 |
頁數 | 4 |
期刊 | Physical Review E - Statistical, Nonlinear, and Soft Matter Physics |
卷 | 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