34 resultados para thermal light
em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"
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Foram sintetizados compostos Ln-L no estado sólido, onde Ln significa os lantanídeos leves trivalentes e L é o piruvato. Estes compostos foram caracterizados e estudados utilizando-se a Termogravimetria e Termogravimetria derivada (TG/DTG), calorimetria exploratória diferencial (DSC) difratometria de raios X pelo método do pó, espectroscopia na região do infravermelho, análise elementar e complexometria. Os resultados permitiram obter informações com respeito a composição, desidratação, sitio de coordenação, comportamento térmico e a decomposição térmica destes compotos.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Monochromatic light excitation in conjunction with thermally stimulated depolarization current measurements are applied to indirect bandgap AlxGa1-xAs. The obtained average activation energy for dipole relaxation is in very close agreement with the DX center binding energy. Monochromatic light induces state transition in the defect and makes possible the identification of dipoles observed in the dark. Charge relaxation currents are destroyed by photoionization of Al0.5Ga0.5As using either 647 nm Kr+ or 488 nm Ar+ laser lines, which are above the DX center threshold photoionization energy. It suggests that correlation may exist among charged donor states DX--d+. Sample resistance as a function of temperature is also measured in the dark and under illumination and shows the probable X valley effective mass state participation in the electron trapping. Ionization with energies of 0.8 eV and 1.24 eV leads to striking current peak shifts in the thermally stimulated depolarization bands. Since vacancies are present in this material, they may be responsible for the secondary band observed in the dark as well as participation in the light induced recombination process.
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This study measured the critical temperature reaching time and also the variation of temperature in the surface of the cervical region and within the pulp chamber of human teeth submitted to dental bleaching using 35% hydrogen peroxide gel activated by three different light sources. The samples were randomly divided into 3 groups (n = 15), according to the catalyst light source: Halogen Light (HL), High Intensity Diode Laser (DL), and Light Emmited Diode (LED). The results of temperature variation were submitted to the analysis of variance and Tukey test with p < 0.05. The temperature increase (mean value and standard deviation) inside the pulp chamber for the HL group was 6.8 ± 2.8°C; for the DL group was 15.3 ± 8.8°C; and for the LED group was 1.9 ± 1.0°C for. The temperature variation (mean value and standard deviation) on the tooth surface, for the group irradiated with HL was 9.1 ± 2.2°C; for the group irradiated with DL were 25.7 ± 18.9°C; and for the group irradiated with LED were 2.6 ± 1.4°C. The mean temperature increase values were significantly higher for the group irradiated with DL when compared with groups irradiated with HL and LED (p < 0.05). When applying the inferior limits of the interval of confidence of 95%, an application time of 38.7 s was found for HL group, and 4.4 s for DL group. The LED group did not achieve the critical temperatures for pulp or the periodontal, even when irradiated for 360 s. The HL and DL light sources may be used for dental bleaching for a short period of time. The LED source did not heat the target tissues significantly within the parameters used in this study. © 2010 Pleiades Publishing, Ltd.
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Solid-state LnL3·1.25H2O compounds, where L is oxamate and Ln is light trivalent lanthanides, have been synthesized. Simultaneous thermogravimetry and differential scanning calorimetry (TG-DSC), experimental and theoretical infrared spectroscopy, TG-DSC coupled to FTIR, elemental analysis, complexometry, and X-ray powder diffractometry were used to characterize and to study the thermal behavior of these compounds. The results led to information about the composition, dehydration, thermal stability, thermal decomposition, and gaseous products evolved during the thermal decomposition of these compounds in dynamic air atmosphere. The dehydration occurs in a single step and through a slow process. The thermal decomposition of the anhydrous compounds occur in a single (Ce), two (Pr), and three (La, Nd to Gd) steps with the formation of the respective oxides, CeO2, Pr 6O11, and Ln2O3 (Ln = La, Nd to Gd). The theoretical and experimental spectroscopic study suggests that the carboxylate group and amide carbonyl group of oxamate are coordinate to the metals in a bidentate chelating mode. © 2012 Akadémiai Kiadó, Budapest, Hungary.
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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.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)