NiTiO3 nanoparticles encapsulated with SiO2 prepared by sol-gel method

NiTiO3 (NTO) nanoparticles encapsulated with SiO2 were prepared by the sol-gel method resulting on core-shell structure. Changes on isoelectric point as a function of silica were evaluated by means of zeta potential. The NTO nanoparticles heat treated at 600 degrees C were characterized by X-ray diffraction, transmission electron microscopy (TEM) and energy dispersive X-ray analysis. TEM observations showed that the mean size of NTO is in the range of 2.5-42.5 nm while the thickness of SiO2 shell attained 1.5-3.5 nm approximately.

Gelation and drying of weakly bonded silica-PPO nanocomposites

Silica-poly(oxypropylene) (PPO) nanocomposites containing PPO with weak physical bonds between the organic (PPO) and inorganic (silica) phases were obtained by the sol-gel procedure. Three precursor sols containing silica and PPO with molecular weights of 1000, 2000 and 4000g/mol were prepared. The structure changes during the whole sol-gel process, i.e. sol formation, sol-gel transition and gel aging and drying were investigated in situ by small angle X-ray scattering (SAXS). The experimental SAXS curves corresponding to sols and wet gels containing PPO of molecular weight 1000g/mol indicate that the aggregates formed during the studied process are fractal objects. Close to the sol-gel transition and during gel aging the fractal dimension is D=2.5. A clearly different structure evolution occurs in samples prepared with PPO with molecular weights 2000 and 4000 g/mol. Our SAXS results indicate the presence of two coexisting and well-defined structure levels, one of them corresponding to small silica clusters and the other to large silica aggregates. These two levels remain along the whole transformation. The SAXS curves of all dry samples are similar to those of the corresponding wet gels suggesting that no significant changes at nanoscopic scale occur during the drying process.

Lanthanum-based perovskites obtained by the polymeric precursor method

Cobalt oxides, specially the ones with perovskite structure, are of a high technological interest, due to their interesting optical, electrical and magnetic properties. La(1 -x)Ca(x)CoO(3) powder samples were synthesized by the polymeric precursor method, with x varying from 0 to 0.4. The powder precursors were characterized by TG/DTA, XRD and IR. The TG curves showed several thermal decomposition steps; the first one is ascribed to the loss of water and the remaining steps are related to the combustion of the organic matter. The XRD patterns indicated only the presence of the perovskite phase. Moreover, the structure changes from rhombohedral to cubic, as calcium is added to the perovskite and the calcination temperature increases.

Comportamento contrátil de barreiras selantes de solo estabilizado para base de lagoas de tratamento

Liners were proposed as subsoil contamination protection devices for waste disposal sites. In the rural environment, they can be used to construct pond bottoms for liquid waste treatment, but the construction needs to be quick and cheap. A good technical solution for these situations is the use of local soil compacted with low quantities of cement or lime, obtaining good properties for this purpose. These barriers need special care about their contraction behavior which may compromise its use. This work shows the results of contraction tests in sandy soil specimens and others stabilized with lime and with cement. Soil structure changes during cure time were checked using electronic scan microscopy. Results show maximum soil contraction of 0.648% for specimen with 14 days cure process. After twenty eight days of cure the contraction values were lower than 0.5%, which classifies the material as of low contraction. Electronic scan image shows significant material structure alteration up to seven days cure. Results show that studied mixtures had appropriate contraction behavior for liner usage.

Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface

The orphan receptor nerve growth factor-induced B (NGFI-B) is a member of the nuclear receptor's subfamily 4A (Nr4a). NGFI-B was shown to be capable of binding both as a monomer to an extended half-site containing a single AAAGGTCA motif and also as a homodimer to a widely separated everted repeat, as opposed to a large number of nuclear receptors that recognize and bind specific DNA sequences predominantly as homo- and/or heterodimers. To unveil the structural organization of NGFI-B in solution, we determined the quaternary structure of the NGFI-B LBD by a combination of ab initio procedures from small-angle X-ray scattering (SAXS) data and hydrogen-deuterium exchange followed by mass spectrometry. Here we report that the protein forms dimers in solution with a radius of gyration of 2.9 nm and maximum dimension of 9.0 nm. We also show that the NGFI-B LBD dimer is V-shaped, with the opening angle significantly larger than that of classical dimer's exemplified by estrogen receptor (ER) or retinoid X receptor (RXR). Surprisingly, NGFI-B dimers formation does not occur via the classical nuclear receptor dimerization interface exemplified by ER and RXR, but instead, involves an extended surface area composed of the loop between helices 3 and 4 and C-terminal fraction of the helix 3. Remarkably, the NGFI-B dimer interface is similar to the dimerization interface earlier revealed for glucocorticoid nuclear receptor (GR), which might be relevant to the recognition of cognate DNA response elements by NGFI-B and to antagonism of NGFI-B-dependent transcription exercised by GR in cells. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society.

Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies

Glossoscolex paulistus (HbGp) hemoglobin is an oligomeric protein, presenting a quaternary structure constituted by 144 globin and 36 non-globin chains (named linkers) with a total molecular mass of 3.6MDa. SDS effects on the oxy-HbGp thermal stability were studied, by DLS and SAXS, at pH 5.0, 7.0 and 9.0. DLS and SAXS data show that the SDS-oxy-HbGp interactions induce a significant decrease of the protein thermal stability, with the formation of larger aggregates, at pH 5.0. At pH 7.0, oxy-HbGp undergoes complete oligomeric dissociation, with increase of temperature, in the presence of SDS. Besides, oxy-HbGp 3.0mg/mL, pH 7.0, in the presence of SDS, has the oligomeric dissociation process reduced as compared to 0.5mg/mL of protein. At pH 9.0, oxy-HbGp starts to dissociate at 20°C, and the protein is totally dissociated at 50°C. The thermal dissociation kinetic data show that oxy-HbGp oligomeric dissociation at pH 7.0, in the presence of SDS, is strongly dependent on the protein concentration. At 0.5mg/mL of protein, the oligomeric dissociation is complete and fast at 40 and 42°C, with kinetic constants of (2.1±0.2)×10-4 and (5.5±0.4)×10-4s-1, respectively, at 0.6mmol/L SDS. However, at 3.0mg/mL, the oligomeric dissociation process starts at 46°C, and only partial dissociation, accompanied by aggregates formation is observed. Moreover, our data show, for the first time, that, for 3.0mg/mL of protein, the oligomeric dissociation, denaturation and aggregation phenomena occur simultaneously, in the presence of SDS. Our present results on the surfactant-HbGp interactions and the protein thermal unfolding process correspond to a step forward in the understanding of SDS effects. © 2013 Elsevier B.V.

Caracterização da interação de inositol hexafosfato e cloreto com hemoglobina humana: aspectos energéticos e estruturais

Pós-graduação em Biofísica Molecular - IBILCE

Estudos conformocionais de diversas proteínas em solução utilizando a técnica de espalhamento de raios-X à baixo ângulo-saxs

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

A teoria dos refúgios florestais e as evidências vegetacionais e litológicas da região sudoeste do município de Corumbá/MS

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Competência em informação na UFPR TV: a inter-relaçâo entre informação, conhecimento e comunicação

Pós-graduação em Ciência da Informação - FFC

Characterization of a Hexameric Exo-Acting GH51 alpha-l-Arabinofuranosidase from the Mesophilic Bacillus subtilis

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Carrying progeny on the back: reproduction in the Brazilian aquatic frog Pipa carvalhoi

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Evolução geomorfológica e palaeoambiental dos terraços da margem esquerda do alto rio Paraná

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Low resolution structural characterization of the Hsp70-interacting protein - Hip - from Leishmania braziliensis emphasizes its high asymmetry

The Hsp70 is an essential molecular chaperone in protein metabolism since it acts as a pivot with other molecular chaperone families. Several co-chaperones act as regulators of the Hsp70 action cycle, as for instance Hip (Hsp70-interacting protein). Hip is a tetratricopeptide repeat protein (TPR) that interacts with the ATPase domain in the Hsp70-ADP state, stabilizing it and preventing substrate dissociation. Molecular chaperones from protozoans, which can cause some neglected diseases, are poorly studied in terms of structure and function. Here, we investigated the structural features of Hip from the protozoa Leishmania braziliensis (LbHip), one of the causative agents of the leishmaniasis disease. LbHip was heterologously expressed and purified in the folded state, as attested by circular dichroism and intrinsic fluorescence emission techniques. LbHip forms an elongated dimer, as observed by analytical gel filtration chromatography, analytical ultracentrifugation and small angle X-ray scattering (SAXS). With the SAXS data a low resolution model was reconstructed, which shed light on the structure of this protein, emphasizing its elongated shape and suggesting its domain organization. We also investigated the chemical-induced unfolding behavior of LbHip and two transitions were observed. The first transition was related to the unfolding of the TPR domain of each protomer and the second transition of the dimer dissociation. Altogether. LbHip presents a similar structure to mammalian Hip, despite their low level of conservation, suggesting that this class of eukaryotic protein may use a similar mechanism of action. (C) 2012 Elsevier Inc. All rights reserved.