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Use of the ising model for doubly ordered macromolecules
Author(s) -
Tenenbaum A.,
Triolo L.
Publication year - 1972
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1972.360110317
Subject(s) - macromolecule , chemistry , ising model , endothermic process , hydrogen bond , chemical physics , side chain , crystallography , helix (gastropod) , statistical physics , molecule , physics , polymer , organic chemistry , biochemistry , adsorption , ecology , snail , biology
We developed a statistical model, based on a one‐dimensional Ising model, for a recently studied polypeptide which displays an endothermic helix‐to‐coil transition with an “anomalous” behavior in the heat of solution. The model supports the assumption of an ordering of the chains due to a specific hydrogen bond interaction among them, beside the helical ordering of the backbone; this double ordering of the macromolecule produces the “anomalous” experimental behavior. With the hypothesis of a highly coopertive interaction among amide groups and side chains, we find that the backbone cooperation increases the chains cooperation, but not vice versa; this influence when the cooperation in the backbone increases.