1997/10/02 by Mohammad Reza Ejtehadi, M. R. Ejtehadi, N. Hamedani +6 · 1 citation
Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #Protein Structure and Dynamics #RNA and protein synthesis mechanisms #cond-mat.soft #q-bio
paper · pdf · doi:10.1088/0305-4470/31/29/006
published as J. Phys. A: Math. Gen. 31 (1998) 6141-6155 · 14 pages, Latex file, 3 latex and 6 eps figures are included
arxiv created 1997/10/02 · openalex publication_date 1998/07/24 · arxiv updated 2009/11/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
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.