Highly designable protein structures and inter-monomer interactions

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Abstract
By exact computer enumeration and combinatorial methods, we have calculated the designability of proteins in a simple lattice hydrophobic-polar 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 the potential. We also show that the existence of a unique ground state is highly sensitive to mutation in certain sites.
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