6533b86dfe1ef96bd12ca903
RESEARCH PRODUCT
Myoglobin on Silica: A Case Study of the Impact of Adsorption on Protein Structure and Dynamics
Serge PinJean-marc ZanottiJean Philippe RenaultCamille LoupiacStéphanie DevineauFabrice NeiersLoussiné Zargariansubject
Isothermal microcalorimetrytrypsin inhibitorCircular dichroismspectroscopySurface Propertiesserum albuminwaterAnalytical chemistrymetmyoglobin02 engineering and technology010402 general chemistry01 natural sciencesCondensed Matter::Materials Sciencechemistry.chemical_compoundAdsorptionProtein structureElectrochemistryAnimalsGeneral Materials Science[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPhysics::Chemical PhysicsQuantitative Biology::BiomoleculesProtein dynamicsnanoparticleneutron scatteringtransitionSurfaces and Interfacesstability021001 nanoscience & nanotechnologyCondensed Matter PhysicsSilicon Dioxide0104 chemical sciencesCondensed Matter::Soft Condensed MatterMyoglobinchemistryMetmyoglobinChemical physicsNanoparticlesThermodynamicsnormal modeAdsorption0210 nano-technologyProtein adsorptiondescription
International audience; If protein structure and function changes upon adsorption are well documented, modification of adsorbed protein dynamics remains a blind spot, despite its importance in biological processes. The adsorption of metmyoglobin on a silica surface was studied by isotherm measurements, microcalorimetry, circular dichroïsm, and UV-visible spectroscopy to determine the thermodynamic parameters of protein adsorption and consequent structure modifications. The mean square displacement and the vibrational densities of states of the adsorbed protein were measured by elastic and inelastic neutron scattering experiments. A decrease of protein flexibility and depletion in low frequency modes of myoglobin after adsorption on silica was observed. Our results suggest that the structure loss itself is not the entropic driving force of adsorption.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2013-10-25 |