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Paper   IPM / P / 6596
School of Physics
  Title:   Stability of Preferable Structures for An HP Model of Protein Folding
1.  M.R. Ejtehadi
2.  N. Hamedani
3.  V. Shahrezaei
4.  H. Seyed Allaei
5.  M. Yahyanejad
  Status:   Published
  Journal: Phys. Rev. E
  No.:  95
  Vol.:  57
  Year:  1998
  Pages:   3298-3301
  Supported by:  IPM
By exact computer enumeration we have calculated the designability of proteins in a simple lattice hydrophobic-polar mode! for the protein folding problem. We show that if the strength of the nonadditive part of the interaction potential becomes larger than a critical value, the degree of designability of structures will depend on the parameters of potential.

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