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Title: Elasticity and Inverse Temperature Transition in Elastin

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.
 [1] ;  [2] ;  [3] ;  [2] ;  [1]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  3. Julich Research Centre (Germany). Julich Centre for Neutron Science (JCNS); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
OSTI Identifier:
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Journal of Physical Chemistry Letters
Additional Journal Information:
Journal Volume: 6; Journal Issue: 20; Journal ID: ISSN 1948-7185
American Chemical Society
Research Org:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; 36 MATERIALS SCIENCE ELP; entropy; hydrophobic hydration; low-frequency vibrations; neutron scattering