Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9675557 | Colloids and Surfaces A: Physicochemical and Engineering Aspects | 2005 | 8 Pages |
Abstract
Small angle X-ray scattering (SAXS) has been performed on native ovalbumin solutions and heated ovalbumin systems at neutral pH and low ionic strength. In native ovalbumin solutions there is a partial ordering, where the interparticle distance (dmax) scales with the protein concentration (C) as dmax â¼Â Câ0.28. This exponent indicates that the ovalbumin monomers behave as a uniform distribution of charged spheres in solution. The q-dependent scattering intensity of ovalbumin aggregates can be well described by a form factor of rods. The dependence of dmax for aggregates on the protein concentration was found to be dmax â¼Â Câ0.51, this scaling behavior is in good agreement with that theoretically derived for the distribution of spaces in a random network of straight fibers. The existence of a well-defined interparticle distance between aggregates is confirmed by cryo-TEM. The scattering profiles of native and aggregated ovalbumin were successfully fitted including both form factor and structure factor, using the preferred distance (L), a measure of disorder (Ï/L), and the radius (R or a) as fitting parameters.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
Mireille Weijers, Els H.A. de Hoog, Martien A. Cohen Stuart, Ronald W. Visschers, Peter A. Barneveld,