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Sökning: WFRF:(Cardinaux Frederic)

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1.
  • Cardinaux, Frederic, et al. (författare)
  • Cluster-Driven Dynamical Arrest in Concentrated Lysozyme Solutions
  • 2011
  • Ingår i: The Journal of Physical Chemistry Part B. - : American Chemical Society (ACS). - 1520-5207 .- 1520-6106. ; 115:22, s. 7227-7237
  • Tidskriftsartikel (refereegranskat)abstract
    • We present a detailed experimental and numerical study of the structural and dynamical properties of salt-free lysozyme solutions. In particular, by combining small-angle X-ray scattering (SAXS) data with neutron spin echo (NSE) and rheology experiments, we are able to identify that an arrest transition takes place at intermediate densities, driven by the slowing down of the cluster motion. Using an effective pair potential among proteins, based on the combination of short-range attraction and long-range repulsion, we account remarkably well for the peculiar volume fraction dependence of the effective structure factor measured by SAXS. We show that a transition from a monomer to a cluster-dominated fluid happens at volume fractions larger than phi greater than or similar to 0.05 where the close agreement between NSE measurements and Brownian dynamics simulations confirms the transient nature of the clusters. Clusters even stay transient above the geometric percolation found in simulation at phi > 0.15, though NSE reveals a cluster lifetime that becomes increasingly large and indicates a divergence of the diffusivity at phi greater than or similar to 0.26. Macroscopic measurements of the viscosity confirm this transition where the long-lived-nature of the clusters is at the origin of the simultaneous dynamical arrest at all length scales.
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2.
  • Gibaud, Thomas, et al. (författare)
  • Phase separation and dynamical arrest for particles interacting with mixed potentials—the case of globular proteins revisited
  • 2011
  • Ingår i: Soft Matter. - : Royal Society of Chemistry (RSC). - 1744-683X .- 1744-6848. ; 7:2, s. 857-860
  • Tidskriftsartikel (refereegranskat)abstract
    • We examine the applicability of the extended law of corresponding states (ELCS) to equilibrium and non equilibrium features of the state diagram of the globular protein lysozyme. We provide compelling evidence that the ELCS correctly reproduces the location of the binodal for different ionic strengths, but fails in describing the location of the arrest line. We subsequently use Mode Coupling Theory (MCT) to gain additional insight into the origin of these observations. We demonstrate that while the critical point and the connected binodal and spinodal are governed by the integral features of the interaction potential described by the normalized second virial coefficient, the arrest line is mainly determined by the attractive well depth or bond strength.
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