Simple model of protein folding kinetics.
- 10 October 1995
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 92 (21), 9801-9804
- https://doi.org/10.1073/pnas.92.21.9801
Abstract
A simple model of the kinetics of protein folding is presented. The reaction coordinate is the "correctness" of a configuration compared with the native state. The model has a gap in the energy spectrum, a large configurational entropy, a free energy barrier between folded and partially folded states, and a good thermodynamic folding transition. Folding kinetics is described by a master equation. The folding time is estimated by means of a local thermodynamic equilibrium assumption and then is calculated both numerically and analytically by solving the master equation. The folding time has a maximum near the folding transition temperature and can have a minimum at a lower temperature.Keywords
This publication has 10 references indexed in Scilit:
- Principles of protein folding — A perspective from simple exact modelsProtein Science, 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
- Kinetics of Protein Folding: A Lattice Model Study of the Requirements for Folding to the Native StateJournal of Molecular Biology, 1994
- The nature of folded states of globular proteinsBiopolymers, 1992
- Levinthal's paradox.Proceedings of the National Academy of Sciences, 1992
- Implications of thermodynamics of protein folding for evolution of primary sequencesNature, 1990
- Metastability of the folded states of globular proteins.Proceedings of the National Academy of Sciences, 1990
- Spin glasses and the statistical mechanics of protein folding.Proceedings of the National Academy of Sciences, 1987