Premium
Dynamic‐elastic investigation of the chemical denaturation of collagen fibers
Author(s) -
Reich S.,
Katchalsky A.,
Oplatka A.
Publication year - 1968
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.1968.360060810
Subject(s) - chemistry , elasticity (physics) , denaturation (fissile materials) , rubber elasticity , macromolecule , natural rubber , biophysics , salt (chemistry) , salt solution , folding (dsp implementation) , polymer chemistry , composite material , biochemistry , materials science , organic chemistry , nuclear chemistry , biology , electrical engineering , engineering
The dynamic elastic behavior of collagen fibers treated by LiBr solutions was studied by the method of free longitudinal vibrations. The frequency response functions and the stress–strain relationship were evaluated for fibers denatured to different extents by various concentrations of the salt solution. The James and Guth model for rubber elasticity was applied to the experimental data. The elastometric parameter β, which is a measure of the degree of folding of the macromolecular chains, was found to decrease on increasing the salt concentration. It might thus serve as a characteristic of the degree of denaturation of fibrillar proteins.