Stability of preferable structures for a hydrophobic-polar model of protein folding
- 1 March 1998
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 57 (3) , 3298-3301
- https://doi.org/10.1103/physreve.57.3298
Abstract
By exact computer enumeration 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 nonadditive part of the interaction potential becomes larger than a critical value, the degree of designability of structures will depend on the parameters of potential.Keywords
This publication has 9 references indexed in Scilit:
- Nature of Driving Force for Protein Folding: A Result From Analyzing the Statistical PotentialPhysical Review Letters, 1997
- Emergence of Preferred Structures in a Simple Model of Protein FoldingScience, 1996
- How accurate must potentials be for successful modeling of protein folding?The Journal of Chemical Physics, 1995
- ‘‘Sequence space soup’’ of proteins and copolymersThe Journal of Chemical Physics, 1991
- Enumeration of all compact conformations of copolymers with random sequence of linksThe Journal of Chemical Physics, 1990
- Dominant forces in protein foldingBiochemistry, 1990
- Origins of structure in globular proteins.Proceedings of the National Academy of Sciences, 1990
- Theory for protein mutability and biogenesis.Proceedings of the National Academy of Sciences, 1990
- Intrachain loops in polymers: Effects of excluded volumeThe Journal of Chemical Physics, 1989