Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 32, Pages 13168-13171Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja303894g
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Funding
- CEA
- CNRS
- UJF
- Agence Nationale de la Recherche [ANR-11-BSV5-027]
- ILL PhD fellowship
- EU [HPRI-2001-50065, RII3-CT-2003-505925]
- UK EPSRC within the ILL-EMBL Deuteration Laboratory [GR/R99393/01, EP/C015452/1]
- European Commission under the 7th Framework Programme through the Research Infrastructures action of the Capacities Programme [CP-CSA_INFRA-2008-1.1.1, 226507-NMI3]
- ERC Advanced Grant scheme
- EPSRC (Cross-disciplinary Interfaces Program)
- Marie Curie International Incoming Fellowship
- EPSRC [EP/C015452/1, EP/H029230/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/H029230/1, EP/C015452/1] Funding Source: researchfish
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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.
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