Conformational Entropy of an Ideal Cross-Linking Polymer Chain

Entropy

Oleg K. Vorov¹  Dennis R. Livesay¹ 

[1] ¹Department of Physics and Optical Science, University of North Carolina at Charlotte, USA ²Department of Computer Science and Bioinformatics Research Center, University of North Carolina at Charlotte, USA

关键词: Conformational entropy;    Mayer expansion;    distance constraints;    cross-linking;    hydrogen bonds;    network rigidity;    protein stability;   

DOI  :  10.3390/e10030285

来源: mdpi

【 摘 要 】

We present a novel analytical method to calculate conformational entropy of ideal cross-linking polymers from the configuration integral by employing a Mayer series expansion. Mayer-functions describing chemical bonds within the chain and for cross-links are sharply peaked over the temperature range of interest, and, are well approximated as statistically weighted Dirac delta-functions that enforce distance constraints. All geometrical deformations consistent with a set of distance constraints are integrated over. Exact results for a contiguous series of connected loops are employed to substantiate the validity of a previous phenomenological distance constraint model that describes protein thermodynamics successfully based on network rigidity.

【 授权许可】

CC BY   
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.