Relaxation in a perfect funnel
- 1 June 1997
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 55 (6) , 7354-7363
- https://doi.org/10.1103/physreve.55.7354
Abstract
We have exactly solved the relaxational dynamics of a model protein that possesses a kinetically perfect funnel-like energy landscape. We find that the dependence of the relaxation time τ on the density of states (DOS) and the energy level spacing distributions of the model displays several main types of behavior depending on the temperature T. This allows us to identify possible generic features of the relaxation. For some ranges of T, τ is insensitive to the density of states; for intermediate values of T it depends on the energy level spacing distribution rather than on the DOS directly, and it becomes gradually more dependent on DOS with increasing temperature; finally, the relaxation can also be determined exclusively by the presence of a deep gap in the energy spectrum rather than by the detailed features of the density of states. We found that the behavior of τ crucially depends on the degeneracy of the energy spectrum. For the special case of exponentially increasing degeneracy, we were able to identify a characteristic temperature that roughly separates the relaxational regimes controlled by energetics and by entropy, respectively. Finally, the validity of our theory is discussed when roughness of energy landscape is added.Keywords
All Related Versions
This publication has 15 references indexed in Scilit:
- Simple model of protein folding kinetics.Proceedings of the National Academy of Sciences, 1995
- The Unfolding Thermodynamics of c-Type Lysozymes: A Calorimetric Study of the Heat Denaturation of Equine LysozymeJournal of Molecular Biology, 1995
- Navigating the Folding RoutesScience, 1995
- The nature of folded states of globular proteinsBiopolymers, 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
- Intermediates and barrier crossing in a random energy model (with applications to protein folding)The Journal of Physical Chemistry, 1989
- Spin glasses and the statistical mechanics of protein folding.Proceedings of the National Academy of Sciences, 1987
- Noninteracting local‐structure model of folding and unfolding transition in globular proteins. I. FormulationBiopolymers, 1981
- Statistical properties of many-particle spectraAnnals of Physics, 1979