A Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity

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dc.contributor.authorGallat, Francois-Xavier
dc.contributor.authorBrogan, Alex P S
dc.contributor.authorFichou, Yann
dc.contributor.authorMcGrath, Nina
dc.contributor.authorMoulin, Martine
dc.contributor.authorHartlein, Michael
dc.contributor.authorCombet, Jerome
dc.contributor.authorWuttke, Joachim
dc.contributor.authorMann, Stephen
dc.contributor.authorZaccai, Giueppe
dc.contributor.authorJackson, Colin
dc.contributor.authorPerriman, Adam W
dc.contributor.authorWeik, Martin
dc.date.accessioned2015-12-07T22:32:51Z
dc.date.issued2012
dc.date.updated2016-02-24T11:34:05Z
dc.description.abstractThe 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.
dc.identifier.issn0002-7863
dc.identifier.urihttp://hdl.handle.net/1885/22995
dc.publisherAmerican Chemical Society
dc.sourceJournal of the American Chemical Society
dc.subjectKeywords: Deuterium labeling; Elastic incoherent neutron scattering; Hydration water; Myoglobin motions; Non-aqueous solvents; Polymer surfactants; Protein dynamics; Protein structures; Solvent free; Bioactivity; Coatings; Deuterium; Hydration; Polymers; Solvents;
dc.titleA Polymer Surfactant Corona Dynamically Replaces Water in Solvent-Free Protein Liquids and Ensures Macromolecular Flexibility and Activity
dc.typeJournal article
local.bibliographicCitation.issue32
local.bibliographicCitation.lastpage13171
local.bibliographicCitation.startpage13168
local.contributor.affiliationGallat, Francois-Xavier, Comissariat a l'Energie Atomique
local.contributor.affiliationBrogan, Alex P S, University of Bristol
local.contributor.affiliationFichou, Yann, Institut de Biologie Structurale, Comissariat a l'Energie Atomique
local.contributor.affiliationMcGrath, Nina, University of Bristol
local.contributor.affiliationMoulin, Martine, Institut Laue-Langevin
local.contributor.affiliationHartlein, Michael, Institut Laue-Langevin
local.contributor.affiliationCombet, Jerome, Institut Laue-Langevin
local.contributor.affiliationWuttke, Joachim, Forschungszentrum Jülich
local.contributor.affiliationMann, Stephen, University of Bristol
local.contributor.affiliationZaccai, Giueppe, Comissariat a l'Energie Atomique
local.contributor.affiliationJackson, Colin, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationPerriman, Adam W, University of Bristol
local.contributor.affiliationWeik, Martin, CEA
local.contributor.authoremailu4040768@anu.edu.au
local.contributor.authoruidJackson, Colin, u4040768
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationu5072968xPUB24
local.identifier.citationvolume134
local.identifier.doi10.1021/ja303894g
local.identifier.scopusID2-s2.0-84865127674
local.identifier.thomsonID000307487200007
local.identifier.uidSubmittedByu5072968
local.type.statusPublished Version

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