Microscopic formulation of the Zimm-Bragg model for the helix-coil transition.
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.
Badasyan
A V
AV
Dipartimento di Chimica Fisica, Universita Ca' Foscari di Venezia, Calle Larga S. Marta DD2137, I-30123 Venezia, Italy. artem.badasyan@unive.it
Giacometti
A
A
Mamasakhlisov
Y Sh
YSh
Morozov
V F
VF
Benight
A S
AS
D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D013696:Temperature
D010455:Peptides