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The role of hydrophobic bonding in collagen fibril formation: A quantitative model
Author(s) -
Wallace Donald
Publication year - 1985
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.360240905
Subject(s) - chemistry , fibril , solubility , hydrophobic effect , polymer , solvent , thermodynamics , phase (matter) , collagen fibril , function (biology) , polymer chemistry , crystallography , chemical engineering , organic chemistry , biophysics , biochemistry , physics , evolutionary biology , biology , engineering
A model has been developed for approximating the free energy of collagen fibril formation (Δ F f ) 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 χ 1 , the polymer–solvent interaction term, is entirely due to hydrophobic effects. χ 1 is estimated from hydrophobic bond energies of amino acid side chains, using the results of Némethy and Scheraga. The temperature dependence of χ 1 is utilized to calculate equilibrium solubilities and Δ F f as a function of temperature.