Elasticity and Inverse Temperature Transition in Elastin
Abstract
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.
- Authors:
-
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Julich Research Centre (Germany). Julich Centre for Neutron Science (JCNS); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1265833
- Grant/Contract Number:
- AC05-00OR22725
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Physical Chemistry Letters
- Additional Journal Information:
- Journal Volume: 6; Journal Issue: 20; Journal ID: ISSN 1948-7185
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 36 MATERIALS SCIENCE; ELP; entropy; hydrophobic hydration; low-frequency vibrations; neutron scattering
Citation Formats
Perticaroli, Stefania, Ehlers, Georg, Jalarvo, Niina, Katsaras, John, and Nickels, Jonathan D. Elasticity and Inverse Temperature Transition in Elastin. United States: N. p., 2015.
Web. doi:10.1021/acs.jpclett.5b01890.
Perticaroli, Stefania, Ehlers, Georg, Jalarvo, Niina, Katsaras, John, & Nickels, Jonathan D. Elasticity and Inverse Temperature Transition in Elastin. United States. https://doi.org/10.1021/acs.jpclett.5b01890
Perticaroli, Stefania, Ehlers, Georg, Jalarvo, Niina, Katsaras, John, and Nickels, Jonathan D. Tue .
"Elasticity and Inverse Temperature Transition in Elastin". United States. https://doi.org/10.1021/acs.jpclett.5b01890. https://www.osti.gov/servlets/purl/1265833.
@article{osti_1265833,
title = {Elasticity and Inverse Temperature Transition in Elastin},
author = {Perticaroli, Stefania and Ehlers, Georg and Jalarvo, Niina and Katsaras, John and Nickels, Jonathan D.},
abstractNote = {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.},
doi = {10.1021/acs.jpclett.5b01890},
journal = {Journal of Physical Chemistry Letters},
number = 20,
volume = 6,
place = {United States},
year = {Tue Sep 22 00:00:00 EDT 2015},
month = {Tue Sep 22 00:00:00 EDT 2015}
}
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Works referencing / citing this record:
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