Highly Designable Protein Structures and Inter Monomer Interactions

Abstract

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.

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

Cited by in corpus (9)

• On Hydrophobicity Correlations in Protein Chains
• Simple Models of the Protein Folding Problem
• Geometrically Reduced Number of Protein Ground State Candidates
• Geometry Selects Highly Designable Structures
• Protein Ground State Candidates in a Simple Model: An Exact Enumeration
• An Analytical Approach to the Protein Designability Problem
• Medium effects on the selection of sequences folding into stable proteins in a simple model
• The Origin of the Designability of Protein Structures
• The Designability of Protein Structures: A Lattice-Model Study using the Miyazawa-Jernigan Matrix