Geometrically Reduced Number of Protein Ground State Candidates

Details Geometrically Reduced Number of Protein Ground State Candidates Geometrically Reduced Number of Protein Ground State Candidates

1998-11-10

arxiv.org/abs/cond-mat/9811127v1

Phys. Rev. Lett 82, 4723 (1999)

Physics

Condensed Matter

Soft Condensed Matter

9 page, 4 ps figures are included

Scientific paper

10.1103/PhysRevLett.82.4723

Geometrical properties of protein ground states are studied using an algebraic approach. It is shown that independent from inter-monomer 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 $L^2$. Moreover, the space of the interaction parameters of the model breaks up into well-defined domains, each corresponding to one ground state candidate, which are separated by sharp boundaries. In addition, by exact enumeration, we show there are some sequences which have one absolute unique native state. These absolute ground states have perfect stability against change of inter-monomer interaction potential.

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