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PubMed1977

Small-angle x-ray scattering study of human serum low-density lipoproteins with differential reactivity for an arterial proteoglycan.

The structure and thermal behavior of human serum low-density lipoproteins showing either a high or a low reactivity against a proteoglycan isolated from human arteries have been found to be different from each other. It is suggested that modifications in the lipoprotein surface structure induced by the physical state of the neutral lipids could modulate the affinity of the macromolecule for the arterial component.

Adult↗
PubMed2005

Small-angle X-ray scattering on solutions of carboxymethylcellulose and bovine serum albumin.

The existence of attractive interaction between CMC and BSA was evidenced in solution at pH higher than the protein isoelectric point by means of SAXS. Mixtures of BSA at 10 x 10(-3) g . mL(-1) and CMC at the concentration range of 1 x 10(-3) g . mL(-1) to 10 x 10(-3) g . mL(-1) were investigated. Upturns in the very low q range revealed the presence of aggregates when the CMC concentration was higher than 2 x 10(-3) g . mL(-1). The comparison between the calculated form factor with the experimental curves at intermediate and long q values indicated that the BSA molecules keep their native form in mixtures with CMC concentrations lower than 5 x 10(-3) g . mL(-1). Therefore, for CMC concentrations higher than 2 x 10(-3) g . mL(-1) the mixtures start to present aggregates and free BSA molecules coexisting in solution.

Animals↗
PubMed1999

Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering.

We have used synchrotron radiation, together with stopped-flow and continuous-flow mixing techniques to monitor refolding of lysozyme at pH 5.2. From data measured at times which range from 14 ms to two seconds, we can monitor changes in the size, the shape and the pair distribution function of the polypeptide chain during the folding process. Comparison of the results with the properties of native and GdmCl-unfolded lysozyme shows that a major chain collapse occurs in the dead-time of mixing. During this process about 50 % of the change in radius of gyration between the unfolded protein and the native state occurs and the polypeptide chain adopts a globular shape. Time-resolved fluorescence spectra of this collapsed state suggest that the hydrophobic side-chains are still highly solvent accessible. A subsequently formed intermediate with helical structure in the alpha-domain is nearly identical in size and shape with native lysozyme and has a solvent-inaccessible hydrophobic core. Despite its native-like properties, this intermediate is only slightly more stable (DeltaG0=-4 kJ/mol) than the collapsed state and still much less stable than native lysozyme (DeltaDeltaG0=36 kJ/mol) at 20 degrees C.

Animals↗
PubMed2001

Microfocus small angle X-ray scattering reveals structural features in archaeological bone samples: detection of changes in bone mineral habit and size.

Microfocus X-ray scattering provides a powerful nondestructive technique capable of providing important information about the size, habit, and arrangement of mineral crystals in bone. The technique is capable of probing textural differences in a sample at a micron scale resolution. The study presented here involved the analysis of a number of archaeological bones by microfocus X-ray scattering at the ESRF Grenoble in order to determine local changes in mineral durability. The results showed that regions of bone with a modified microscopic morphology contained a greater dispersion of crystal shape when compared with more intact regions and control contemporary bone samples, but the crystal thickness values showed similar consistency. We speculate that the persistence of collagen in the archaeological bone may allow diagenetic remodeling of bone in terms of crystallite shape but defines the size of remodelled crystallites. The ability to detect such local changes in texture has wide potential for determining crystal characteristics in healthy and diseased bone samples.

Archaeology↗