Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 344318
Title Heat-induced formation of ordered structures of ovalbumin at low ionic strength studied by small angle X-ray scattering
Author(s) Weijers, M.; Hoog, E.H.A. de; Cohen Stuart, M.A.; Visschers, R.W.; Barneveld, P.A.
Source Colloids and Surfaces. A: Physicochemical and Engineering Aspects 270-271 (2005)1-3. - ISSN 0927-7757 - p. 301 - 308.
Department(s) Physical Chemistry and Colloid Science
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) neutron-scattering - induced denaturation - light-scattering - aqueous colloids - globular protein - ph - aggregation - molecules - gels
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 d max ~ C-0.28. 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 ~ C-0.51, 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 (¿/L), and the radius (R or a) as fitting parameters.
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