X-ray small angle scattering experiments, using a pin hole SAXS camera with Synchrotron radiation source, have been performed to study the conformational changes of lyophilized samples of Apo-, Mono-, and Diferric- human transferrin. We report the experimental evidence that the analysis of the scattered intensity through the fractal theory may give information on the particle size and its variation upon iron binding.
Titolo: | X-ray small angle scattering of the human transferrin protein aggregates: A fractal study |
Autori: | |
Data di pubblicazione: | 1993 |
Rivista: | |
Abstract: | X-ray small angle scattering experiments, using a pin hole SAXS camera with Synchrotron radiation source, have been performed to study the conformational changes of lyophilized samples of Apo-, Mono-, and Diferric- human transferrin. We report the experimental evidence that the analysis of the scattered intensity through the fractal theory may give information on the particle size and its variation upon iron binding. |
Handle: | http://hdl.handle.net/11697/16416 |
Appare nelle tipologie: | 1.1 Articolo in rivista |
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