Elasticity and Inverse Temperature Transition in Elastin [electronic resource].

Published:: Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description:: pages 4,018-4,025 : digital, PDF file
Additional Creators:: Oak Ridge National Laboratory, United States. Department of Energy. Office of Basic Energy Sciences, and United States. Department of Energy. Office of Scientific and Technical Information

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Summary:

Structurally, elastin is protein and biomaterial that provides elasticity and resilience to a range of tissues. This work provides insights into the elastic properties of elastin and its peculiar inverse temperature transition (ITT). These features are dependent on hydration of elastin and are driven by a similar mechanism of hydrophobic collapse to an entropically favorable state. Moreover, when using neutron scattering, we quantify the changes in the geometry of molecular motions above and below the transition temperature, showing a reduction in the displacement of water-induced motions upon hydrophobic collapse at the ITT. Finally, we measured the collective vibrations of elastin gels as a function of elongation, revealing no changes in the spectral features associated with local rigidity and secondary structure, in agreement with the entropic origin of elasticity.

Report Numbers:

E 1.99:1265833

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Published through SciTech Connect.
09/22/2015.
"KC0402010"
"ERKCSNX"
Journal of Physical Chemistry Letters 6 20 ISSN 1948-7185 AM
Stefania Perticaroli; Georg Ehlers; Niina Jalarvo; John Katsaras; Jonathan D. Nickels.

Funding Information:

AC05-00OR22725

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