Highly Designable Protein Structures and Inter Monomer Interactions

Details Highly Designable Protein Structures and Inter Monomer Interactions Highly Designable Protein Structures and Inter Monomer Interactions

1997-10-02

arxiv.org/abs/cond-mat/9710028v1

J. Phys. A: Math. Gen. 31 (1998) 6141-6155

Physics

Condensed Matter

Soft Condensed Matter

14 pages, Latex file, 3 latex and 6 eps figures are included

Scientific paper

10.1088/0305-4470/31/29/006

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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