Microscopic formulation of the Zimm-Bragg model for the helix-coil transition

Abstract

A microscopic spin model is proposed for the phenomenological Zimm-Bragg model for the helix-coil transition in biopolymers. This model is shown to provide the same thermophysical properties of the original Zimm-Bragg model and it allows a very convenient framework to compute statistical quantities. Physical origins of this spin model are made transparent by an exact mapping into a one-dimensional Ising model with an external field. However, the dependence on temperature of the reduced external field turns out to differ from the standard one-dimensional Ising model and hence it gives rise to different thermophysical properties, despite the exact mapping connecting them. We discuss how this point has been frequently overlooked in the recent literature.

11 pages, 2 figures

References in corpus (2)

• An Ising-Like model for protein mechanical unfolding
• Kinetics of the helix-coil transition

Cited by in corpus (18)

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• Crowding effect on helix-coil transition: beyond entropic stabilization
• Solvent Effects in the Helix-Coil Transition Model can explain the Unusual Biophysics of Intrinsically Disordered Proteins
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• Statistical mechanics of DNA-nanotube adsorption
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• Zero temperature phase transitions and their anomalous influence on thermodynamic behavior in the q-state Potts model on a diamond chain
• Spectral mechanism and nearly reducible transfer matrices for pseudotransitions in one-dimensional systems
• Thermal transitions in a one-dimensional, finite-size Ising model