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Folding of a 16-residue helical peptide using molecular dynamics simulation with Tsallis effective potential

Journal of Chemical Physics, ISSN: 0021-9606, Vol: 111, Issue: 10, Page: 4359-4361
1999
  • 36
    Citations
  • 0
    Usage
  • 9
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    36
    • Citation Indexes
      36
  • Captures
    9

Article Description

We have demonstrated that a molecular dynamics simulation method in conjunction with a Tsallis effective potential enables a 16-residue model peptide to fold into a complete α-helix in a reasonably short time. The current study also indicates that one can practically observe reversible foldings of the peptide with the method, mainly due to its superior capability of overcoming potential energy barriers. Therefore it is anticipated that the new method may provide a quite efficient conformational searching tool for systems with many degrees of freedom such as proteins and DNAs. © 1999 American Institute of Physics.

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