title: Elasticity and Inverse Temperature Transition in Elastin.
abstract: Elastin is a structural 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. 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. We also 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.
authors.affiliation: Joint Institute for Neutron Sciences, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.|Chemical and Materials Sciences Division, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.|Department of Chemistry, University of Tennessee , Knoxville, Tennessee 37996, United States.
authors.forename: Stefania
authors.initials: S
authors.lastname: Perticaroli
authors.affiliation: Quantum Condensed Matter Division, Oak Ridge National Laboratory , P.O. Box 2008, Oak Ridge, Tennessee 37831, United States.
authors.forename: Georg
authors.initials: G
authors.lastname: Ehlers
authors.affiliation: Jülich Centre for Neutron Science (JCNS), Forschungszentrum Jülich , D-52425 Jülich, Germany.|Chemical and Engineering Materials Division, Neutron Sciences Directorate, and JCNS Outstation at the Spallation Neutron Source (SNS), Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.
authors.forename: Niina
authors.initials: N
authors.lastname: Jalarvo
authors.affiliation: Joint Institute for Neutron Sciences, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.|Biology and Soft Matter Division, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.
authors.forename: John
authors.initials: J
authors.lastname: Katsaras
authors.affiliation: Joint Institute for Neutron Sciences, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.|Biology and Soft Matter Division, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37831, United States.|The Department of Physics and Astronomy, University of Tennessee, Knoxville , Knoxville, Tennessee 37996, United States.
authors.forename: Jonathan D
authors.initials: JD
authors.lastname: Nickels
mesh_terms: D004548:Elasticity; D004549:Elastin / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D033363:Neutron Diffraction; D012542:Scattering, Radiation; D017550:Spectroscopy, Fourier Transform Infrared; D044366:Transition Temperature; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D004549:Elastin
keywords: ELP; entropy; hydrophobic hydration; low-frequency vibrations; neutron scattering