TY  - JOUR
AU  - Perticaroli, Stefania
AU  - Ehlers, Georg
AU  - Jalarvo, Niina
AU  - Katsaras, John
AU  - Nickels, Jonathan D.
TI  - Elasticity and Inverse Temperature Transition in Elastin
JO  - The journal of physical chemistry letters
VL  - 6
SN  - 1948-7185
CY  - Washington, DC
PB  - ACS
M1  - FZJ-2015-05802
SP  - 4018–4025
PY  - 2015
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000363083900005
C6  - pmid:26722771
DO  - DOI:10.1021/acs.jpclett.5b01890
UR  - https://juser.fz-juelich.de/record/255669
ER  -