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Paper   IPM / Physic / 6617
School of Physics
  Title:   Geometrically Reduced Number of Protein Ground State Condidates
1.  M.R. Ejtehadi
2.  N. Hamedani
3.  V. Shahrezaei
  Status:   Published
  Journal: Phys. Rev. Lett.
  No.:  51
  Vol.:  82
  Year:  1999
  Pages:   4723-4726
  Supported by:  IPM
Geometrical properties of protein ground states are studied using an algebraic approach. It is shown that independent from intermonomer interactions, the collection of ground state candidates for any folded protein is unexpectedly small: For the case of a two-parameter hydrophobic-polar lattice model for L-mers, the number of these candidates grows only as L2. Moreover, by exact enumeration, we show there are some sequences which have one absolute unique native state. These absolute ground states have perfect stability against any change of intermonomer interaction potential.

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