arXiv · cond-mat/9710028
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.
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M. R. Ejtehadi, N. Hamedani, H. Seyed-Allaei, V. Shahrezaei, M. Yahyanejad. 1997-10-02. Highly Designable Protein Structures and Inter Monomer Interactions. https://doi.org/10.1088/0305-4470%2F31%2F29%2F006
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