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Diffusive dynamics of ordered solutions of apoferritin near the structure factor peak
14
Citations
22
References
2002
Year
Protein ChemistryBiochemistryProtein FoldingMedicineNatural SciencesExperimental BiophysicsBiophysical AspectMolecular BiologyOrdered SolutionsStructural BiologySpherical ShellConformational StudyMolecular BiophysicsStructure Factor PeakSolution Nmr SpectroscopyAqueous SolutionsBiophysicsDiffusive Dynamics
Aqueous solutions of apoferritin, which consists of 24 proteins assembled into a spherical shell (outer diameter 12 nm), represent highly monodisperse systems. In low-salt solutions, a pronounced peak in the static structure factor S(q) indicates intermolecular interactions due to the net negative charge (pH ≈ 5) of apoferritin. We have investigated both the structure and dynamics of ordered solutions for the first time in the vicinity of the S(q) peak at q*. Coherent small-angle neutron scattering experiments were performed at the Institute Laue-Langevin (Grenoble) and the dynamics was studied using the high-resolution neutron spin echo spectrometer IN15. The dynamics at q > q* coincides with extrapolated results of previous experiments. For low-salt solutions, the normalized intermediate-scattering function has a shape that qualitatively resembles that of S(q) in the vicinity of q*. However, the inverse effective diffusion constant differs quantitatively from S(q) below q*.
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