949 resultados para quaternary structure changes


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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Aim To assess (i) heat generated by pluggers during warm vertical compaction of gutta-percha and investigation of temperature changes on the external root surface during canal filling, and (ii) the chemical changes of root canal sealers induced by heat.Methodology Four sealers, namely AH Plus, MTA Plus and two other experimental sealers based on tricalcium silicate, were characterised. External temperatures generated on the root surface during warm vertical compaction of gutta-percha with different sealers inside the root canal were monitored using an infrared thermography camera. Chemical changes induced by heating the sealers were assessed by Fourier transform infrared (FT-IR) spectroscopy.Results MTA Plus and the experimental sealers were composed of a cement and radiopacifier, with epoxy resin or a water-soluble polymer as dispersant, whilst AH Plus was epoxy resin-based. The heat generated at the tips of the continuous wave pluggers was found to be lower than the temperature set and indicated on the device LCD display. The sealers reduced the heat generated on the external root surfaces during the heating phase. AH Plus sustained changes to its chemical structure after exposure to heat, whilst the other sealers were unaffected.Conclusions The temperatures recorded at the tips of continuous wave pluggers varied with their taper and were lower than the temperature set on the System B LCD display. Root canal sealers reduced the dissipation of heat generated during warm vertical compaction, with the temperature at the external root surface maintained at 37-41 degrees C, a temperature below that is necessary to cause irreversible damage to bone and periodontium. The use of AH Plus sealer during warm vertical compaction techniques results in chemical changes in the sealer. The effect on sealer properties needs to be further investigated.

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The objective of this study was to evaluate the structure of Tanzania grassland grazed by goats managed with different residue leaf area index (RLAI) under intermittent stocking. The experiment was carried out from February to August, 2008. The treatments consisted of three different targets RLAI (0.8, 1.6 and 2.4) and 95% light interception (LI) criterion determined the rest period. Forage samples were collected at average height sampling points and weighed. Subsequently, a smaller sample was removed to separate the morphological components (leaf, stem and dead material) and to determine the structural and productive features. The canopy architecture was evaluated by the method of inclined point quadrat. The pre-grazing height in the paddocks were significantly different among treatments. RLAI influenced dry matter contents of green forage, leaf, stem and total, with the exception of dry matter of dead material, where the lowest values were observed for 0.8 RLAI. Thus, RLAI modifies canopy structure and is sensitive to canopy height changes throughout the year. Pasture regrowth is not compromised by residual leaf area indexes between 0.8 and 2.4, when climatic factors are not limiting.

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Chromatoid body (CB) is a typical cytoplasmic organelle of germ cells, and it seems to be involved in RNA/protein accumulation for later germ-cell differentiation. Despite most of the events in mammals spermatogenesis had been widely described in the past decades and the increase in the studies related to the CB molecular composition and physiology, the origins and functions of this important structure of male germ cells are still unclear. The aims of this study were to describe the nucleolar cycle and also to find some relationship between the nucleolar organization and the CB assembling during the spermatogenesis in mammals. Cytochemical and cytogenetics analysis showed nucleolar fragmentation in post-pachytene spermatocytes and nucleolar reorganization in post-meiotic spermatids. Significant difference in the number and in the size of nucleoli between spermatogonia and round spermatids, as well as differences in the nucleolar position within the nucleus were also observed. Ultrastructural analysis showed the CB assembling in the cytoplasm of primary spermatocytes and the nucleolar fragmentation occurring at the same time. In conclusion our results suggest that the CB may play important roles during the spermatogenesis process in mammals and that its origin may be related to the nucleolar cycle during the meiotic cell cycle.

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The N-terminus of the human dihydroorotate dehydrogenase (HsDHODH) has been described as important for the enzyme attachment in the inner mitochondrial membrane and possibly to regulate enzymatic activity. In this study, we synthesized the peptide acetyl-GDERFYAEHLMPTLQGLLDPESAHRL AVRFTSLGamide, comprising the residues 33-66 of HsDHODH N-terminal conserved microdomain. Langmuir monolayers and circular dichroism (CD) were employed to investigate the interactions between the peptide and membrane model, as micelles and monolayers of the lipids phosphatidylcholine (PC), 3-phosphatidylethanolamine (PE) and cardiolipin (CL). These lipids represent the major constituents of inner mitochondrial membranes. According to CD data, the peptide adopted a random structure in water, whereas it acquired α-helical structures in the presence of micelles. The π–A isotherms and polarization- modulated infrared reflection-absorption spectroscopy on monolayers showed that the peptide interacted with all lipids, but in different ways. In DPPC monolayers, the peptide penetrated into the hydrophobic region. The strongest initial interaction occurred with DPPE, but the peptide was expelled from this monolayer at high surface pressures. In CL, the peptide could induce a partial dissolution of the monolayer, leading to shorter areas at the monolayer collapse. These results corroborate the literature, where the HsDHODH microdomain is anchored into the inner mitochondrial membrane. Moreover, the existence of distinct conformations and interactions with the different membrane lipids indicates that the access to the enzyme active site may be controlled not only by conformational changes occurring at the microdomain of the protein, but also by some lipid-protein synergetic mechanism, where the HsDHODH peptide would be able to recognize lipid domains in the membrane. - See more at: http://www.eurekaselect.com/122062/article#sthash.1ZZbc7E0.dpuf

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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