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@ARTICLE{Gallat:22578,
author = {Gallat, F.-X. and Brogan, A.P.S. and Fichou, Y. and
McGrath, N. and Moulin, M. and Härtlein, M. and Combet, J.
and Wuttke, J. and Mann, S. and Zaccai, G. and Jackson, C.J.
and Perriman, A.W. and Weik, M.},
title = {{A} {P}olymer {S}urfactant {C}orona {D}ynamically
{R}eplaces {W}ater in {S}olvent-{F}ree {P}rotein {L}iquids
and {E}nsures {M}acromolecular {F}lexibility and {A}ctivity},
journal = {Journal of the American Chemical Society},
volume = {134},
issn = {0002-7863},
address = {Washington, DC},
publisher = {American Chemical Society},
reportid = {PreJuSER-22578},
pages = {13168},
year = {2012},
note = {The authors thank the ILL, the FRMII, and the Diamond Light
Source for beamtime. We thank Bernhard Frick for his
continuous support related to IN16 experiments and Douglas
Tobias for critical reading of an early version of the
manuscript. Financial support by the CEA, the CNRS, and the
UJF is acknowledged, as well as a grant from the Agence
Nationale de la Recherche (ANR-11-BSV5-027) to M.W. and an
ILL PhD fellowship to F.-X.G. This work has benefited from
the activities of the DLAB consortium funded by the EU
(HPRI-2001-50065 and RII3-CT-2003-505925) and from UK
EPSRC-funded activity within the ILL-EMBL Deuteration
Laboratory (GR/R99393/01 and EP/C015452/1). The study has
been supported by the European Commission under the 7th
Framework Programme through the "Research Infrastructures"
action of the "Capacities" Programme
$(CP-CSA_INFRA-2008-1.1.1$ No. 226507-NMI3) and ERC Advanced
Grant scheme (S.M.). We thank the EPSRC (Cross-disciplinary
Interfaces Program) for support for AWP. C.J.J. was
supported by a Marie Curie International Incoming
Fellowship.},
abstract = {The observation of biological activity in solvent-free
protein-polymer surfactant hybrids challenges the view of
aqueous and nonaqueous solvents being unique promoters of
protein dynamics linked to function. Here, we combine
elastic incoherent neutron scattering and specific deuterium
labeling to separately study protein and polymer motions in
solvent-free hybrids. Myoglobin motions within the hybrid
are found to closely resemble those of a hydrated protein,
and motions of the polymer surfactant coating are similar to
those of the hydration water, leading to the conclusion that
the polymer surfactant coating plasticizes protein
structures in a way similar to hydration water.},
keywords = {J (WoSType)},
cin = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
Science JCNS (München) ; JCNS-FRM-II / JCNS-1},
ddc = {540},
cid = {I:(DE-Juel1)ICS-1-20110106 /
I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106},
pnm = {BioSoft: Makromolekulare Systeme und biologische
Informationsverarbeitung (FUEK505) / 544 - In-house Research
with PNI (POF2-544) / NMI3 - Integrated Infrastructure
Initiative for Neutron Scattering and Muon Spectroscopy
(226507)},
pid = {G:(DE-Juel1)FUEK505 / G:(DE-HGF)POF2-544 /
G:(EU-Grant)226507},
experiment = {EXP:(DE-MLZ)SPHERES-20140101},
shelfmark = {Chemistry, Multidisciplinary},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22853639},
UT = {WOS:000307487200007},
doi = {10.1021/ja303894g},
url = {https://juser.fz-juelich.de/record/22578},
}