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The low- temperature mechanical relaxation of elastin. II. The solvated protein

✍ Scribed by M. Scandola; G. Pezzin

Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
485 KB
Volume
17
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The low‐temperature dynamic mechanical relaxation of ox Ligamentum nuchae elastin, swollen with water and ethylene glycol at various swelling ratios, has been investigated by means of the Rheovibron DDV II viscoelastometer, at frequencies from 3.5 to 110 Hz. The peak location on the temperature scale, its intensity and activation energy have been studied as a function of solvent content and it has been found that the two solvents influence the dynamic mechanical behavior in a quite different way. A similar interaction of the solvent molecules with the backbone peptide groups is assumed for both solvents, and the differences in the mechanical spectra, which are more marked the higher the solvation degree, are explained in terms of the different size of the protein–solvent relaxing units.

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