Statistical Physics of Biopolymer Conformations

A special issue of Polymers (ISSN 2073-4360). This special issue belongs to the section "Polymer Physics and Theory".

Deadline for manuscript submissions: closed (30 November 2021) | Viewed by 2961

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Materials Research Laboratory, University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia
Interests: theory of conformational transitions in biopolymers
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Special Issue Information

Dear Colleagues,

Polymers are molecules comprised of many repeating subunits. This fact rationalizes the application of Statistical Mechanics to achieve the physical description at the level of a single macromolecule, which is already a statistical system on its own. The phase space of the problem is very rich thanks to the existence of many possible microstates for each subunit (monomer), leading to the statistical ensemble of polymer conformations. Torsional or dihedral angles which play the role of generalized coordinates, are hindered: the energy profile usually has several minima, referred to as isomeric states or isomers. The fact that most of the time monomers are found in one of few isomeric states, leads to the Rotational Isomeric State (RIS) approximation and discretization of coordinate values. This is the regular logic behind the spin model applications in Polymer Physics.

Although the above is true for both synthetic and natural polymers, when it comes to the polypeptides and polynucleotides, the publications are often more directed towards the biologically inspired interpretation of obtained theoretical results.

This Special Issue is intended for papers reporting important advances in statistical mechanical models and approaches, describing order-disorder (helix-coil, protein denaturation, DNA melting, etc.) transitions in biopolymers from the viewpoint of physics. Approaches related to the account of solvent-related effects are especially welcome.

Dr. Artem Badasyan
Guest Editor

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Keywords

  • Biopolymer
  • polypeptide
  • polynucleotide
  • protein folding
  • helix-coil transition
  • DNA melting
  • cold denaturation
  • water-protein interactions
  • Ising model
  • Potts model
  • Zimm-Bragg model
  • Lifson-Roig model
  • Wako-Saito-Munoz-Eaton model

Published Papers (1 paper)

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11 pages, 571 KiB  
Article
System Size Dependence in the Zimm–Bragg Model: Partition Function Limits, Transition Temperature and Interval
by Artem Badasyan
Polymers 2021, 13(12), 1985; https://doi.org/10.3390/polym13121985 - 17 Jun 2021
Cited by 4 | Viewed by 2192
Abstract
Within the recently developed Hamiltonian formulation of the Zimm and Bragg model we re-evaluate several size dependent approximations of model partition function. Our size analysis is based on the comparison of chain length N with the maximal correlation (persistence) length ξ of helical [...] Read more.
Within the recently developed Hamiltonian formulation of the Zimm and Bragg model we re-evaluate several size dependent approximations of model partition function. Our size analysis is based on the comparison of chain length N with the maximal correlation (persistence) length ξ of helical conformation. For the first time we re-derive the partition function of zipper model by taking the limits of the Zimm–Bragg eigenvalues. The critical consideration of applicability boundaries for the single-sequence (zipper) and the long chain approximations has shown a gap in description for the range of experimentally relevant chain lengths of 5–10 persistence lengths ξ. Correction to the helicity degree expression is reported. For the exact partition function we have additionally found, that: at N/ξ10 the transition temperature Tm reaches its asymptotic behavior of infinite N; the transition interval ΔT needs about a thousand persistence lengths to saturate at its asymptotic, infinite length value. Obtained results not only contribute to the development of the Zimm–Bragg model, but are also relevant for a wide range of Biotechnologies, including the Biosensing applications. Full article
(This article belongs to the Special Issue Statistical Physics of Biopolymer Conformations)
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