Static and Dynamic Scattering of β-Lactoglobulin Aggregates Formed after Heat-Induced Denaturation at pH 2
| Autor: | Pierre Aymard, Taco Nicolai, Dominique Durand, Allan H. Clark |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Persistence length
chemistry.chemical_classification Polymers and Plastics Chemistry Scattering Globular protein Organic Chemistry Analytical chemistry Ionic bonding Light scattering Inorganic Chemistry Ionic strength Materials Chemistry Physical chemistry Denaturation (biochemistry) Structure factor |
| Zdroj: | Macromolecules. 32:2542-2552 |
| ISSN: | 1520-5835 0024-9297 |
| DOI: | 10.1021/ma981689j |
| Popis: | The structure and internal dynamics of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2 and different ionic strengths were investigated using light, neutron, and X-ray scattering. Polydisperse aggregates are formed with a rigid rodlike local structure with mass per unit length close to that of a string of β-lactoglobulin monomers but with a somewhat larger diameter. The persistence length decreases with increasing ionic strength from more than 600 nm at 0.013 M to 38 nm at 0.1 M. At ionic strengths of 0.1 and 0.2 M, a self-similar structure with fractal dimensions of 1.8 and 2.0 is seen by using light scattering. The concentration dependence of the static structure factor and the internal dynamics are close to those of flexible linear chains. In contrast, a rigid behavior is observed at lower ionic strength (0.03 and 0.013 M). The persistence length of aggregates formed at 0.013 M is reduced after dilution in 0.1 and 0.2 M ionic strength solvents but remains larger than that of ag... |
| Databáze: | OpenAIRE |
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