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| Home > Publications database > A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity > print |
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| 024 | 7 | _ | |2 pmid |a pmid:22853639 |
| 024 | 7 | _ | |2 DOI |a 10.1021/ja303894g |
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| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Gallat, F.-X. |b 0 |
| 245 | _ | _ | |a A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity |
| 260 | _ | _ | |a Washington, DC |b American Chemical Society |c 2012 |
| 300 | _ | _ | |a 13168 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
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| 440 | _ | 0 | |0 25743 |a Journal of the American Chemical Society |v 134 |y 32 |
| 500 | _ | _ | |a 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. |
| 520 | _ | _ | |a 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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| 856 | 7 | _ | |u http://dx.doi.org/10.1021/ja303894g |
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