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The role of hydrophobic bonding in collagen fibril formation: A quantitative model

✍ Scribed by Donald Wallace

Publisher
Wiley (John Wiley & Sons)
Year
1985
Tongue
English
Weight
891 KB
Volume
24
Category
Article
ISSN
0006-3525

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✦ Synopsis

Synopsis

A model has been developed for approximating the free energy of collagen fibril formation (AF,) and the equilibrium solubility of collagen under physiological conditions. The model utilizes an expression of Flory for rodlike polymers, with the modification that the "pure" anisotropic phase is defined as a collagen fibril containing about 0.3 g water/g collagen. The model also assumes that xl, the polymer-solvent interaction term, is entirely due to hydrophobic effects. x1 is estimated from hydrophobic bond energies of amino acid side chains, using the results of Nemethy and Scheraga. The temperature dependence of xI is utilized to calculate equilibrium solubilities and AF, as a function of temperature.

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## Abstract An analysis of the available data on the thermostability and imino acid content of various collagens has shown that the change of the denaturation temperature (__t__~__m__~) of the collagen triple helix, as well as the temperature of hydrothermic shrinkage (__t__~__s__~) of collagen fib