Counterions release from electrostatic complexes of polyelectrolytes and proteins of opposite charge : a direct measurement

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dc.creatorGummel, Jérémie
dc.creatorCousin, Fabrice
dc.creatorBoué, François
dc.date2009-04-06
dc.date.accessioned2026-07-07T13:00:46Z
dc.date.available2026-07-07T13:00:46Z
dc.descriptionThough often considered as one of the main driving process of the complexation of species of opposite charges, the release of counterions has never been experimentally directly measured on polyelectrolyte/proteins complexes. We present here the first structural determination of such a release by Small Angle Neutron Scattering in complexes made of lysozyme, a positively charged protein and of PSS, a negatively charged polyelectrolyte. Both components have the same neutron density length, so their scattering can be switched off simultaneously in an appropriate "matching" solvent; this enables determination of the spatial distribution of the single counterions within the complexes. The counterions (including the one subjected to Manning condensation) are expelled from the cores where the species are at electrostatic stoichiometry.
dc.identifierhttps://arxiv.org/abs/0904.0858
dc.identifierhttp://arxiv.org/abs/0904.0858
dc.identifierJournal of American Chemical Society / JACS 129, 18 (2007) 5806-5807
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/225946
dc.subjectChemical Physics
dc.titleCounterions release from electrostatic complexes of polyelectrolytes and proteins of opposite charge : a direct measurement
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