{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T12:50:52Z","timestamp":1762865452643,"version":"build-2065373602"},"reference-count":32,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2008,9,20]],"date-time":"2008-09-20T00:00:00Z","timestamp":1221868800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Entropy"],"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.3390\/e10030285","type":"journal-article","created":{"date-parts":[[2008,9,29]],"date-time":"2008-09-29T05:43:40Z","timestamp":1222667020000},"page":"285-308","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Conformational Entropy of an Ideal Cross-Linking Polymer Chain"],"prefix":"10.3390","volume":"10","author":[{"given":"Oleg K.","family":"Vorov","sequence":"first","affiliation":[{"name":"Department of Physics and Optical Science, University of North Carolina at Charlotte, USA"}]},{"given":"Dennis R.","family":"Livesay","sequence":"additional","affiliation":[{"name":"Department of Computer Science and Bioinformatics Research Center, University of North Carolina at Charlotte, USA"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7711-1639","authenticated-orcid":false,"given":"Donald J.","family":"Jacobs","sequence":"additional","affiliation":[{"name":"Department of Physics and Optical Science, University of North Carolina at Charlotte, USA"}]}],"member":"1968","published-online":{"date-parts":[[2008,9,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1021\/bi00327a032","article-title":"Theory for the folding and stability of globular proteins","volume":"24","author":"Dill","year":"1985","journal-title":"Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding","volume":"29","author":"Dill","year":"1990","journal-title":"Biochemistry"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3924","DOI":"10.1016\/S0006-3495(03)75120-0","article-title":"A Measure of Conformational Entropy Change during Thermal Protein Unfolding Using Neutron Spectroscopy","volume":"84","author":"Fitter","year":"2003","journal-title":"Biophys. 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