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Use of the ising model for doubly ordered macromolecules

โœ Scribed by A. Tenenbaum; L. Triolo


Publisher
Wiley (John Wiley & Sons)
Year
1972
Tongue
English
Weight
496 KB
Volume
11
Category
Article
ISSN
0006-3525

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โœฆ Synopsis


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 side chains due t o a specific hydrogen bond interaction among them, beside the helical ordering of the backbone; this double ordering of the macromolecule produces the %nomalous" experimental behavior. With the hypot.hesis of a highly cooperative interaction among amide groups of the backbone, of a slightly cooperative interaction among side chains, and of no interaction among amide groups and side chains, we find that the backbone cooperation increases the chains cooperation, but not vice versa; this influence decreases when the cooperat,ion in the backbone increases.


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