Correlated energy landscape model for finite, random heteropolymers
- 1 June 1996
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 53 (6) , 6271-6296
- https://doi.org/10.1103/physreve.53.6271
Abstract
In this paper, we study the role of correlations in the energy landscape of a finite random heteropolymer by developing the mapping onto the generalized random energy model (GREM) proposed by Derrida and Gardner [J. Phys. C 19, 2253 (1986)] in the context of spin glasses. After obtaining the joint distribution for energies of pairs of configurations, and by calculating the entropy of the polymer subject to weak and strong topological constraints, the model yields thermodynamic quantities such as ground-state energy, entropy per thermodynamic basin, and glass transition temperature as functions of the polymer length and packing density. These are found to be very close to the uncorrelated landscape or random energy model (REM) estimates. A tricritical point is obtained where behavior of the order parameter q changes from first order with a discrete jump at the transition, to second-order continuous. While the thermodynamic quantities obtained from the free energy are close to the REM values, the Levinthal entropy describing the number of basins which must be searched at the glass transition is significantly modified by correlations. © 1996 The American Physical Society.Keywords
This publication has 41 references indexed in Scilit:
- Toward an outline of the topography of a realistic protein-folding funnel.Proceedings of the National Academy of Sciences, 1995
- 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
- Proteins with selected sequences fold into unique native conformationPhysical Review Letters, 1994
- Protein folding funnels: a kinetic approach to the sequence-structure relationship.Proceedings of the National Academy of Sciences, 1992
- Optimal protein-folding codes from spin-glass theory.Proceedings of the National Academy of Sciences, 1992
- Spin glasses and the statistical mechanics of protein folding.Proceedings of the National Academy of Sciences, 1987
- Theoretical Studies of Protein FoldingAnnual Review of Biophysics and Bioengineering, 1983
- Random-energy model: An exactly solvable model of disordered systemsPhysical Review B, 1981