Abstract
The low-temperature dielectric relaxation of collagen and elastin was studied over a wide range of hydrations h. The hydration-shell response increases weakly with temperature, is thermally activated, and conforms to energy barrier scaling. This demonstrates the existence of a decoupled, secondary relaxation akin to that in binary structural glasses. Indications for fragile-to-strong transitions and other changes of mechanism are not found for hydrated collagen and elastin. For low h, the dielectric strength increases superlinearly with h; concomitantly, the water molecules trigger significant mobility of the protein surface.
Original language | English |
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Pages (from-to) | 12628-12631 |
Number of pages | 4 |
Journal | Journal of Physical Chemistry B |
Volume | 113 |
Issue number | 38 |
DOIs | |
State | Published - Sep 24 2009 |
Externally published | Yes |