Is Heteropolymer Freezing Well Described by the Random Energy Model?
- 20 May 1996
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 76 (21) , 3987-3990
- https://doi.org/10.1103/physrevlett.76.3987
Abstract
It is widely held that the random energy model (REM) describes the freezing transition of a variety of types of heteropolymers. We demonstrate that the hallmark property of REM, statistical independence of the energies of states over disorder, is violated in different ways for models commonly employed in heteropolymer freezing studies. The implications for proteins are also discussed.Keywords
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This publication has 20 references indexed in Scilit:
- How accurate must potentials be for successful modeling of protein folding?The Journal of Chemical Physics, 1995
- Funnels, pathways, and the energy landscape of protein folding: A synthesisProteins-Structure Function and Bioinformatics, 1995
- Folding kinetics of proteinlike heteropolymersThe Journal of Chemical Physics, 1994
- When is a potential accurate enough for structure prediction? Theory and application to a random heteropolymer model of protein foldingThe Journal of Chemical Physics, 1994
- Inverse protein folding problem: designing polymer sequences.Proceedings of the National Academy of Sciences, 1992
- Influence of point mutations on protein structure: Probability of a neutral mutationJournal of Theoretical Biology, 1991
- Formation of unique structure in polypeptide chainsBiophysical Chemistry, 1989
- Frozen states of a disordered globular heteropolymerJournal of Physics A: General Physics, 1989
- Spin glasses and the statistical mechanics of protein folding.Proceedings of the National Academy of Sciences, 1987
- Random-Energy Model: Limit of a Family of Disordered ModelsPhysical Review Letters, 1980