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1.
J Chem Phys ; 132(16): 164515, 2010 Apr 28.
Artículo en Inglés | MEDLINE | ID: mdl-20441296

RESUMEN

The parameters of fullerene C(60) dissolved in carbon disulfide CS(2) are analyzed by small-angle neutron scattering (SANS) in a wide interval of momentum transfer. To exclude the influence of nonequilibrium conditions, the solutions are prepared without applying shaking, stirring or ultrasound. No indication of the equilibrium cluster state of C(60) (with the cluster size below 60 nm) in the final solutions is revealed. Molecular dynamic simulations are complementary used to find out the partial volume of C(60) in CS(2) and the scattering contribution of the solvent organization at the interface with the fullerene molecule, which is shown to be small. Among several approaches for describing SANS data the preference is given to the model, which takes into account the presence of stable C(60) dimers (comprising 10% of the total particle number density) in the solution.

2.
Biochemistry (Mosc) ; 75(11): 1324-30, 2010 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-21314599

RESUMEN

The structure of the oligomeric protein α-crystallin from bovine eye lens was investigated by small-angle neutron scattering (SANS) with contrast variation. Based on the SANS curves, the match point for α-crystallin (43% D2O) and its average scattering length density at this point (2.4·10(10) cm(-2)) were evaluated. The radius of gyration and the distance distribution functions for α-crystallin were calculated. On the basis of these calculations, it was concluded that α-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration, and all polypeptide subunits in α-crystallin oligomers undergo equal deuteration. The latter indicates that all α-crystallin subunits are equally accessible for water and presumably for some other low molecular weight substances. These conclusions on the α-crystallin structure (homogeneous distribution of scattering density and equal accessibility of all subunits for low molecular weight substances) should be taken into account when elaborating α-crystallin quaternary structure models.


Asunto(s)
alfa-Cristalinas/química , Algoritmos , Animales , Bovinos , Medición de Intercambio de Deuterio , Difracción de Neutrones , Estructura Cuaternaria de Proteína , Estructura Terciaria de Proteína , Dispersión del Ángulo Pequeño , Propiedades de Superficie
3.
J Colloid Interface Sci ; 295(1): 100-7, 2006 Mar 01.
Artículo en Inglés | MEDLINE | ID: mdl-16102775

RESUMEN

Results of experiments on small-angle neutron scattering from ferrofluids on polar carriers (pentanol, water, methyl-ethyl-ketone), with double-layer sterical stabilization of magnetic nanoparticles, are reported. Several types of spatial structural organization are observed. The structure of highly stable pentanol-based samples is similar to that of stable ferrofluids based on organic non-polar carriers (e.g., benzene) with mono-layer covered magnetic nanoparticles. At the same time, the effect of the interparticle interaction on the scattering is stronger in polar ferrofluids because of the structural difference in the surfactant shell. The structure of the studied methyl-ethyl-ketone- and water-based ferrofluids essentially different from the previous case. The formation of large (>100 nm in size) elongated or fractal aggregates, respectively, is detected even in the absence of external magnetic field, which corresponds to weaker stability of these types of ferrofluids. The structure of the fractal aggregates in water-based ferrofluids does not depend on the particle concentration, but it is sensitive to temperature. A temperature increase results in a decrease in their fractal dimension reflecting destruction of the aggregates. In addition, in water-based ferrofluids these aggregates consist of small (radius approximately 10 nm) and temperature-stable primary aggregates.


Asunto(s)
Hierro/química , Magnetismo , Nanopartículas del Metal/química , Difracción de Neutrones , Dispersión del Ángulo Pequeño , Coloides
4.
J Pharm Biomed Anal ; 114: 288-91, 2015 Oct 10.
Artículo en Inglés | MEDLINE | ID: mdl-26093243

RESUMEN

Phospholipid transport nanosystem (PTNS) for drug delivery is based on soybean phosphatidylcholine. The morphology of PTNS is investigated by means of small-angle X-ray scattering. The obtained results allow one to answer the key question from the viewpoint of organization of drug incorporation whether the PTNS nanoparticles have a structure of micelles or vesicles. It is demonstrated that PTNS is a vesicular system with an average vesicle radius of 160 ± 2Å.


Asunto(s)
Portadores de Fármacos , Glycine max/química , Nanopartículas/química , Fosfatidilcolinas/química , Sistemas de Liberación de Medicamentos , Emulsiones , Membrana Dobles de Lípidos/química , Micelas , Dispersión de Radiación , Solventes , Rayos X
5.
J Colloid Interface Sci ; 334(1): 37-41, 2009 Jun 01.
Artículo en Inglés | MEDLINE | ID: mdl-19376524

RESUMEN

The structure of ferrofluids (magnetite in decahydronaphtalene) stabilized with saturated mono-carboxylic acids of different chain lengths (lauric, myristic, palmitic and stearic acids) is studied by means of magnetization analysis and small-angle neutron scattering. It is shown that in case of saturated acid surfactants, magnetite nanoparticles are dispersed in the carrier approximately with the same size distribution whose mean value and width are significantly less as compared to the classical stabilization with non-saturated oleic acid. The found thickness of the surfactant shell around magnetite is analyzed with respect to stabilizing properties of mono-carboxylic acids.

6.
Langmuir ; 20(11): 4363-8, 2004 May 25.
Artículo en Inglés | MEDLINE | ID: mdl-15969139

RESUMEN

Highly stable and reproducible molecular-colloidal water solutions of C60 fullerenes (FWS) obtained by transferring fullerenes from an organic solution into an aqueous phase with the help of ultrasonic treatment are investigated by means of small-angle neutron scattering (SANS). A polydispersity in the size of detected particles up to 84 nm is revealed. These particles are slightly anisotropic and have a characteristic size of approximately 70 nm. Along with it, there are some indications that a significant part of fullerenes composes particles with the size of the order of 1 nm. The contrast variation based on mixtures of light and heavy water shows that the mean scattering length density of the particles is close to that of the packed fullerene associates as well as that the characteristic size of possible fluctuations of the scattering length density within the particles does not exceed 2 nm. A smooth surface resulting in the Porod law for the scattering is detected. A number of models discussed in the literature are considered with respect to the SANS data.

7.
Biochemistry ; 41(51): 15342-9, 2002 Dec 24.
Artículo en Inglés | MEDLINE | ID: mdl-12484773

RESUMEN

The conformation of mammalian elongation factor eEF1A in solution was examined by the small angle neutron scattering and scanning microcalorimetry. We have found that in contrast to the bacterial analogue the eEF1A molecule has no fixed rigid structure in solution. The radius of gyration of the eEF1A molecule (5.2 nm) is much greater than that of prokaryotic EF1A. The specific heat of denaturation is considerably lower for eEF1A than for EF1A, suggesting that the eEF1A conformation is significantly more disordered. Despite its flexible conformation, eEF1A is found to be highly active in different functional tests. According to the neutron scattering data, eEF1A becomes much more compact in the complex with uncharged tRNA. The absence of a rigid structure and the possibility of large conformational change upon interaction with a partner molecule could be important for eEF1A functioning in channeled protein synthesis and/or for the well-known capability of the protein to interact with different ligands besides the translational components.


Asunto(s)
Factor 1 de Elongación Peptídica/química , Animales , Proteínas Bacterianas/química , Proteínas Bacterianas/fisiología , Calorimetría/métodos , Guanosina Difosfato/química , Neutrones , Biosíntesis de Péptidos , Factor 1 de Elongación Peptídica/análogos & derivados , Factor 1 de Elongación Peptídica/fisiología , Conformación Proteica , Estructura Terciaria de Proteína , Aminoacil-ARN de Transferencia/química , Conejos , Dispersión de Radiación , Soluciones , Thermus thermophilus
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