Published In
Physical Review E
Document Type
Article
Publication Date
5-2011
Subjects
Biopolymers -- Physiological transport, Biopolymers, Solvents -- Hydrogen bonding
Abstract
The problem of the helix-coil transition of biopolymers in explicit solvents, such as water, with the ability for hydrogen bonding with a solvent is addressed analytically using a suitably modified version of the Generalized Model of Polypeptide Chains. Besides the regular helix-coil transition, an additional coil-helix or reentrant transition is also found at lower temperatures. The reentrant transition arises due to competition between polymer-polymer and polymer-water hydrogen bonds. The balance between the two types of hydrogen bonding can be shifted to either direction through changes not only in temperature, but also by pressure, mechanical force, osmotic stress, or other external influences. Both polypeptides and polynucleotides are considered within a unified formalism. Our approach provides an explanation of the experimental difficulty of observing the reentrant transition with pressure and underscores the advantage of pulling experiments for studies of DNA. Results are discussed and compared with those reported in a number of recent publications with which a significant level of agreement is obtained.
DOI
10.1103/PhysRevE.83.051903
Persistent Identifier
http://archives.pdx.edu/ds/psu/7151
Citation Details
Badasyan, A. V., Tonoyan, S. A., Mamasakhlisov, Y. S., Giacometti, A., Benight, A. S., & Morozov, V. F. (2011). Competition for hydrogen-bond formation in the helix-coil transition and protein folding. [Article]. Physical Review E, 83(5), 9
Description
This is the publisher's final pdf. Article appears in Physical Review E (http://pre.aps.org/) and is copyrighted by APS Journals (http://publish.aps.org/)