Abstract
The effect of hydration on phase composition, aminoacids side-chain dynamics, and domain thickness of hard α-keratin was investigated by 1H solid-state NMR. Decomposition of wide-line 1H NMR spectra was used to determine the phase composition and to obtain information on molecular motion. Proton spin-diffusion NMR experiments using a double-quantum dipolar filter were used to estimate the rigid domain sizes for the hydrated Caucasian hair fibres. The relative domain sizes were obtained from the solution of spin-diffusion equation for cylindrical morphologies in the initial-rate approximation by a novel approach. A qualitative model describing the morphological and molecular dynamics changes induced by hydration was developed.
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