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

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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
Volume6
Issue number2
DOIs
Publication statusPublished - 2007 Jun 1

Fingerprint

folding
Peptides
peptides
Molecular dynamics
molecular dynamics
Disulfides
Computer simulation
disulfides
Denaturation
simulation
biopolymer denaturation
encounters
Experiments
interactions

Keywords

  • Computation
  • Kinetics
  • Protein

ASJC Scopus subject areas

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

Cite this

Molecular dynamics simulation of folding of a short helical toxin peptide. / Tsai, Yi Len; Chen, Hwung Wen; Lin, Topp; Wang, Wei Zhou; Sun, Ying Chieh.

In: Journal of Theoretical and Computational Chemistry, Vol. 6, No. 2, 01.06.2007, p. 213-221.

Research output: Contribution to journalArticle

Tsai, Yi Len ; Chen, Hwung Wen ; Lin, Topp ; Wang, Wei Zhou ; Sun, Ying Chieh. / Molecular dynamics simulation of folding of a short helical toxin peptide. In: Journal of Theoretical and Computational Chemistry. 2007 ; Vol. 6, No. 2. pp. 213-221.
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