Please use this identifier to cite or link to this item: https://doi.org/10.1103/PhysRevE.79.051922
Title: Thermodynamic stability of small-world oscillator networks: A case study of proteins
Authors: Ren, J.
Li, B. 
Issue Date: 27-May-2009
Citation: Ren, J., Li, B. (2009-05-27). Thermodynamic stability of small-world oscillator networks: A case study of proteins. Physical Review E - Statistical, Nonlinear, and Soft Matter Physics 79 (5) : -. ScholarBank@NUS Repository. https://doi.org/10.1103/PhysRevE.79.051922
Abstract: We study vibrational thermodynamic stability of small-world oscillator networks by relating the average mean-square displacement S of oscillators to the eigenvalue spectrum of the Laplacian matrix of networks. We show that the cross-links suppress S effectively and there exist two phases on the small-world networks: (1) an unstable phase: when p□1/N, S∼N; (2) a stable phase: when p□1/N, S∼ p-1, i.e., S/N∼ E cr -1. Here, p is the parameter of small-world, N is the number of oscillators, and Ecr =pN is the number of cross-links. The results are exemplified by various real protein structures that follow the same scaling behavior S/N∼ E cr -1 of the stable phase. We also show that it is the "small-world" property that plays the key role in the thermodynamic stability and is responsible for the universal scaling S/N∼ E cr -1, regardless of the model details. © 2009 The American Physical Society.
Source Title: Physical Review E - Statistical, Nonlinear, and Soft Matter Physics
URI: http://scholarbank.nus.edu.sg/handle/10635/98384
ISSN: 15393755
DOI: 10.1103/PhysRevE.79.051922
Appears in Collections:Staff Publications

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