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@ARTICLE{Perticaroli:255669,
author = {Perticaroli, Stefania and Ehlers, Georg and Jalarvo, Niina
and Katsaras, John and Nickels, Jonathan D.},
title = {{E}lasticity and {I}nverse {T}emperature {T}ransition in
{E}lastin},
journal = {The journal of physical chemistry letters},
volume = {6},
issn = {1948-7185},
address = {Washington, DC},
publisher = {ACS},
reportid = {FZJ-2015-05802},
pages = {4018–4025},
year = {2015},
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.},
cin = {Neutronenstreuung ; JCNS-1 / ICS-1 / JCNS-SNS},
ddc = {530},
cid = {I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-1-20110106 /
I:(DE-Juel1)JCNS-SNS-20110128},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551) /
6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
/ 6215 - Soft Matter, Health and Life Sciences (POF3-621)},
pid = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
G:(DE-HGF)POF3-6215},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000363083900005},
pubmed = {pmid:26722771},
doi = {10.1021/acs.jpclett.5b01890},
url = {https://juser.fz-juelich.de/record/255669},
}