http://www.mdpi.com/journal/entropy/special_issues/entropies_of_polymers/ Related Special Issues in other Journals Entropies of Polymers in Polymers Submission All papers should be submitted to entropy@mdpi.com with copy to the guest editor. To be published continuously until the deadline and papers will be listed together at the special websites. Both, research articles and review articles are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editors for announcment on this website. Submitted papers should not have been published previously, nor be under consideration for publication elsewhere. All papers are refereed through a peer-review process. A guide for authors, sample copies and other relevant information for submitting papers are available on the Instructions for Authors page. Entropy is an international peer-reviewed quarterly journal published by MDPI. Please visit the Instructions for Authors page before submitting a paper. Open Access publication fees are 800 CHF per paper. English correction fees (250 CHF) will be added in certain cases (1050 CHF per paper for those papers that require extensive additional formatting and/or English corrections.). List of Related Papers See a list of related papers on configurational entropy compiled by Shu-Kun Lin http://www.mdpi.com/1099-4300/12/4/961/ One of the most important questions in molecular biology is what determines folding pathways: native structure or protein sequence. There are many proteins that have similar structures but very different sequences, and a relevant question is whether such proteins have similar or different folding mechanisms. To explain the differences in folding rates of various proteins, the search for the factors affecting the protein folding process goes on. Here, based on known experimental data, and using theoretical modeling of protein folding based on a capillarity model, we demonstrate that the relation between the average conformational entropy and the average energy of contacts per residue, that is the entropy capacity, will determine the possibility of the given chain to fold to a particular topology. The difference in the folding rate for proteins sharing more ball-like and less ball-like folds is the result of differences in the conformational entropy due to a larger surface of the boundary between folded and unfolded phases in the transition state for proteins with a more ball-like fold. The result is in agreement with the experimental folding rates for 67 proteins. Proteins with high or low side chain entropy would have extended unfolded regions and would require some additional agents for complete folding. Such proteins are common in nature, and their structural properties are of biological importance. http://www.mdpi.com/1099-4300/12/4/961/ Fri, 16 Apr 2010 00:00:00 CEST Entropy 2010-04-16 12 4 Review 961 982 1099-4300 Influence of Conformational Entropy on the Protein Folding Rate 2010-04-16 doi: 10.3390/e12040961 Galzitskaya http://www.mdpi.com/1099-4300/11/4/907/ The dynamics and statics of flexible polymer chains are based on their conformational entropy, resulting in the properties of isolated polymer chains with any branching potentially being characterized by Gaussian chain models. According to the graph-theoretical approach, the dynamics and statics of Gaussian chains can be expressed as a set of eigenvalues of their Laplacian matrix. As such, the existence of Laplacian cospectral trees allows the structural nonidentifiability of any branched flexible polymer. http://www.mdpi.com/1099-4300/11/4/907/ Fri, 20 Nov 2009 00:00:00 CET Entropy 2009-11-20 11 4 Article 907 916 1099-4300 On the Structural Non-identifiability of Flexible Branched Polymers 2009-11-20 doi: 10.3390/e11040907 Koh-hei Nitta http://www.mdpi.com/1099-4300/10/3/285/ 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. http://www.mdpi.com/1099-4300/10/3/285/ Sat, 20 Sep 2008 00:00:00 CEST Entropy 2008-09-20 10 3 Article 285 308 1099-4300 Conformational Entropy of an Ideal Cross-Linking Polymer Chain 2008-09-20 doi: 10.3390/e10030285 Oleg K. Vorov Dennis R. Livesay Donald J. Jacobs