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Paper   IPM / P / 6597
School of Physics
  Title:   Highly Designable Protein Structures and Inter Monomer Interactions
  Author(s): 
1.  M.R. Ejtehadi
2.  N. Hamedani
3.  H. Seyed Allaei
4.  V. Shahrezaei
5.  M. Yahyanejad
  Status:   Published
  Journal: J. Phys. A: Math. Gen.
  No.:  28
  Vol.:  31
  Year:  1998
  Pages:   6141-6155
  Supported by:  IPM
  Abstract:
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 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. We also show that the existence of a unique ground state is highly sensitive to mutation in certain sites.

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