Dielectric response of deeply supercooled hydration water in the connective tissue proteins collagen and elastin.
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.
Gainaru
Catalin
C
Fakultät for Physik, Technische Universität Dortmund, 44221 Dortmund, Germany. catalin.gainaru@uni-dortmund.de
Fillmer
Ariane
A
Böhmer
Roland
R
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D003238:Connective Tissue / Q000737:chemistry*; D004549:Elastin / Q000737:chemistry*; D013710:Tendons / Q000737:chemistry; D014867:Water / Q000737:chemistry*
D014867:Water; D003094:Collagen; D004549:Elastin