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Paper   IPM / Physic / 7149
School of Physics
  Title:   Preferred Structures and Monomer-Monomer Interaction
1.  N. Hamedani
2.  M. Yahyanejad
3.  H. Seyed Allaei
4.  V. Shahrezaei
5.  M.R. Ejtehadi
  Status:   In Proceedings
  Proceeding: Proc. Mont Carlo approach to Biopolymers and protein folding
  Year:  1998
  Supported by:  IPM
By exact computer enumeration and combinatorial methods, we have calculated the designability of proteins in a simple lattice. H-P model for the protein folding problem. We have used an intermonomer potential which has an additive plus a nonadditive part. This choice facilitates exact enumerations, especially when only the additive potential is present. We show that if the strength of the non-additive part of the interaction potential becomes larger than a critical value, the degree of designability of structures will depend on the parameters of potential. Besides, the strength of the nonadditive part can be used to control the energy gaps. We also show that the existence of a unique ground state is highly sensitive to mutation in certain sites. PACS:82.20.Wt, 36.20.−r, 36.20.Ey, 82.20.Db.

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