Cooperativity and stability in a Langevin model of proteinlike folding
- 8 June 1997
- journal article
- Published by AIP Publishing in The Journal of Chemical Physics
- Vol. 106 (22) , 9276-9285
- https://doi.org/10.1063/1.474039
Abstract
We present two simplified models of protein dynamics based on Langevin’s equation of motion in a viscous medium. We explore the effect of the potential energy function’s symmetry on the kinetics and thermodynamics of simulated folding. We find that an isotropic potential energy function produces, at best, a modest degree of cooperativity. In contrast, a suitable anisotropic potential energy function delivers strong cooperativity.Keywords
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This publication has 22 references indexed in Scilit:
- Theoretical studies of protein-folding thermodynamics and kineticsCurrent Opinion in Structural Biology, 1997
- Folding kinetics of proteinlike heteropolymersThe Journal of Chemical Physics, 1994
- Transition states and folding dynamics of proteins and heteropolymersThe Journal of Chemical Physics, 1994
- Proteins with selected sequences fold into unique native conformationPhysical Review Letters, 1994
- How does a protein fold?Nature, 1994
- Monte Carlo Simulation of a First-Order Transition for Protein FoldingThe Journal of Physical Chemistry, 1994
- The nature of folded states of globular proteinsBiopolymers, 1992
- Metastability of the folded states of globular proteins.Proceedings of the National Academy of Sciences, 1990
- Principles that Govern the Folding of Protein ChainsScience, 1973