Thermal denaturation of hydrated wool keratin by 1H solid-state NMR

Maria Baias, Dan E. Demco, Crisan Popescu, Radu Fechete, Claudiu Melian, Bernhard Blümich, Martin Möller

Research output: Contribution to journalArticle

Abstract

Thermal denaturation of hydrated keratin in wool was investigated by NMR using 1H wide-line spectra to obtain the phase composition and 1H spin-diffusion experiments using a double-quantum filter to obtain the domain sizes for the wool fibers. The denaturation process detected by DSC takes place for wool fibers in deuterated water in the temperature range 140-144 *C. The phase composition measured by 1H wide line NMR spectra reveals a rigid, semirigid and an amorphous phase for temperatures in the range 25-160 *C. A dramatic change in the phase composition was detected around 142 *C, corresponding to the denaturation temperature. The morphological domain sizes measured by 1H spin-diffusion NMR experiments were obtain from the solutions of the spin-diffusion equations for two-dimensional rectangular and cylindrical morphologies. The keratin mobility gradient in the interfacial region at different denaturation temperatures was measured from the 1H spin-diffusion data. A qualitative model describing the denaturation process of hydrated keratin protein was developed that explains the changes in domain thickness, spin diffusivities, phase composition, and thermodynamic parameters.

Original languageEnglish (US)
Pages (from-to)2184-2192
Number of pages9
JournalJournal of Physical Chemistry B
Volume113
Issue number7
DOIs
StatePublished - Feb 19 2009

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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    Baias, M., Demco, D. E., Popescu, C., Fechete, R., Melian, C., Blümich, B., & Möller, M. (2009). Thermal denaturation of hydrated wool keratin by 1H solid-state NMR. Journal of Physical Chemistry B, 113(7), 2184-2192. https://doi.org/10.1021/jp8094616