Abstract
Dynamic infrared linear dichroism (DIRLD) spectroscopy is used to study time-dependent changes in human-hair keratin films under small-amplitude oscillatory strain. The amplitude and rate of submolecular reorientation observed are very dependent on the molecular environment of the functional group being probed. DIRLD spectra of keratin films are extremely sensitive to molecular-level changes induced by temperature, relative humidity, and the addition of hair-treatment actives. By using correlation analysis, DIRLD data can be represented in a two-dimensional infrared (2D IR) format to compare the reorientation rates of individual dipole-transition moments. 2D IR spectra provide a clear resolution enhancement of the naturally broad amide I and amide II IR absorbance bands. The net result is an improved molecular-level understanding of the mechanical properties of human hair and identification of factors affecting these properties.
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