title: X-ray small angle scattering of the human transferrin protein aggregates. A fractal study.
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.
authors.affiliation: Dipartimento di Fisica Universita La Sapienza, Roma, Italy.
authors.forename: A C
authors.initials: AC
authors.lastname: Castellano
authors.forename: M
authors.initials: M
authors.lastname: Barteri
authors.forename: A
authors.initials: A
authors.lastname: Bianconi
authors.forename: E
authors.initials: E
authors.lastname: Borghi
authors.forename: L
authors.initials: L
authors.lastname: Cassiano
authors.forename: M
authors.initials: M
authors.lastname: Castagnola
authors.forename: S
authors.initials: S
authors.lastname: Della Longa
mesh_terms: D001059:Apoproteins / Q000737:chemistry; D006801:Humans; D008956:Models, Chemical; D010316:Particle Size; D011487:Protein Conformation; D012542:Scattering, Radiation; D014168:Transferrin / Q000737:chemistry*; D014965:X-Rays
chemical_list: D001059:Apoproteins; D014168:Transferrin; C028284:apotransferrin; C028283:diferric transferrin