Lattice model of transmembrane polypeptide folding

C. M. Chen*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


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.

Original languageEnglish
Article number010901
Pages (from-to)109011-109014
Number of pages4
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Issue number1 I
Publication statusPublished - 2001

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics


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