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

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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.

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