Stability Threshold as a Selection Principle for Protein Design
- 19 May 1997
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 78 (20) , 3967-3970
- https://doi.org/10.1103/physrevlett.78.3967
Abstract
The sensitivity of the native states of proteinlike heteropolymers to mutations modeled as perturbations in the interaction potential between amino acids is studied. The stability threshold against mutations is shown to be zero for random heteropolymers on a lattice in two dimensions, whereas a design procedure modeling evolution produces a nonzero threshold. We introduce an evolutionlike protein design procedure based on an optimization of the stability threshold that is shown to naturally ensure thermodynamic stability as well.Keywords
All Related Versions
This publication has 25 references indexed in Scilit:
- Criterion that Determines the Foldability of ProteinsPhysical Review Letters, 1996
- New Algorithm for Protein DesignPhysical Review Letters, 1996
- How accurate must potentials be for successful modeling of protein folding?The Journal of Chemical Physics, 1995
- Navigating the Folding RoutesScience, 1995
- Funnels, pathways, and the energy landscape of protein folding: A synthesisProteins-Structure Function and Bioinformatics, 1995
- How does a protein fold?Nature, 1994
- Engineering of stable and fast-folding sequences of model proteins.Proceedings of the National Academy of Sciences, 1993
- The Protein Folding ProblemPhysics Today, 1993
- Formation of unique structure in polypeptide chainsBiophysical Chemistry, 1989
- Principles that Govern the Folding of Protein ChainsScience, 1973