Molecular dynamics simulation of folding of a short helical toxin peptide

Yi Len Tsai, Hwung Wen Chen, Topp Lin, Wei Zhou Wang, Ying Chieh Sun*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


A molecular dynamics simulation of the folding of a short helical toxin peptide was carried out. The simulation gave a folding time of ∼10 ns, which is longer than typical time of ∼1 ns for the formation of 1-2 helical turns. The simulation demonstrates that a helical peptide with disulfide bonds, which may encounter extra steric hindrance compared with the peptide without disulfide bonds, can fold in nanosecond timescale. An analysis shows that this folding time should correspond to the folding time in weak denaturation condition in experiment. Interactions and factors affecting folding pathways are analyzed and discussed.

Original languageEnglish
Pages (from-to)213-221
Number of pages9
JournalJournal of Theoretical and Computational Chemistry
Issue number2
Publication statusPublished - 2007 Jun


  • Computation
  • Kinetics
  • Protein

ASJC Scopus subject areas

  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics


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