RESUMO
The structure of mitochondrial cristas has been studied for the first time by the method of small-angle scattering of thermal neutrons. Experiments were performed on intact functioning rat liver mitochondria. Mitochondrial cristas are usually considered as folds of the internal membrane with arbitrary nonfixed intermembrane distances. It was shown that, under particular conditions, during low-amplitude swelling of mitochondria, cristas are transformed to bimembrane structures, with the distance between the central planes of membranes of 190 E. It was found that the formation of bimembrane structures and their structural parameters do not depend on the method of induction of swelling, by placing the mitochondria into a hypotonic medium or by the opening of nonspecific pores.
Assuntos
Mitocôndrias Hepáticas/ultraestrutura , Membranas Mitocondriais/ultraestrutura , Difração de Nêutrons , Espalhamento a Baixo Ângulo , Animais , Óxido de Deutério/química , Proteínas Mitocondriais/ultraestrutura , Dilatação Mitocondrial , RatosRESUMO
Arrangement of chromatin in intact chicken erythrocyte nuclei was investigated by small angle neutron scattering. The scattering spectra have revealed that on the scales between 15 nm and 1.5 microm the interior of the nucleus exhibited properties of a mass fractal. The fractal dimension of the protein component of cell nucleus held constant at approximately 2.5, while the DNA organization was biphasic, with the fractal dimension slightly higher than 2 on the scales smaller than 300 nm and approaching 3 on the larger scales.
Assuntos
Núcleo Celular/genética , Cromatina/química , Cromatina/genética , DNA/química , Eritrócitos/citologia , Fractais , Conformação de Ácido Nucleico , Animais , Núcleo Celular/química , Galinhas/genética , DNA/metabolismo , Interfase , Difração de NêutronsRESUMO
The filament structures of the self-polymers of RecA proteins from Escherichia coli and Pseudomonas aeruginosa, their complexes with ATPgammaS, phage M13 single-stranded DNA (ssDNA) and the tertiary complexes RecA::ATPgammaS::ssDNA were compared by small angle neutron scattering. A model was developed that allowed for an analytical solution for small angle scattering on a long helical filament, making it possible to obtain the helical pitch and the mean diameter of the protein filament from the scattering curves. The results suggest that the structure of the filaments formed by these two RecA proteins, and particularly their complexes with ATPgammaS, is conservative.
