## Abstract The conformational changes and aggregation process of β‐lactoglobulin (β‐LG) subjected to gamma irradiation are presented. β‐LG in solutions of different protein concentrations (3 and 10 mg/ml) and in solid state with different water activities (a~w~) (0.22; 0.53; 0.74) was irradiated u
Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation
✍ Scribed by Rita Carrotta; Rogert Bauer; Rianne Waninge; Christian Rischel
- Book ID
- 111753401
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2008
- Tongue
- English
- Weight
- 110 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0961-8368
- DOI
- 10.1110/ps.42501
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Small‐angle x‐ray scattering was used for studying intermediate species, isolated after heat‐induced aggregation of the A variant of bovine β‐lactoglobulin. The intermediates were separated in two fractions, the heated metastable dimer and heated metastable oligomers larger than the dim
Adsorption onto chromium surfaces during heat treatment (65-68°C) of beta-lactoglobulin A and B in phosphate buffer, pH 6.88, was investigated by in situ ellipsometry. Thermal unfolding and in situ heat-induced aggregation under the same conditions were studied by differential scanning calorimetry a