“School of Physics”
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| Paper IPM / P / 7149 |
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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 have used an
intermonomer potential which has an additive plus a nonadditive
part. This choice facilitates exact enumerations, especially when
only the additive potential is present. 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. Besides,
the strength of the nonadditive part can be used to control the
energy gaps. We also show that the existence of a unique ground
state is highly sensitive to mutation in certain sites.
PACS:82.20.Wt, 36.20.−r, 36.20.Ey, 82.20.Db.
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