901 resultados para Innovation. Triple helix. Micro and small enterprises


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After thirty two years in Brazil and retired from Universidade Estadual de Campinas the author wishes to present this account, a summary of a large part of the research in synthetic methodology developed by the research groups of Albert J. Kascheres and the author at Universidade Estadual de Campinas Chemistry Institute. Contributions have been made to the area of enaminones, diazocarbonyls, cyclopropenones and azirines.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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To assess the structural and functional significance of the N helix (residues 3-13) of avian recombinant troponin C (rTnC), we have constructed NHdel, in which residues 1-11 have been deleted, both in rTnC and in the spectral probe mutant F29W (Pearlstone, J. R., Borgford, T., Chandra, M., Oikawa, K., Kay, C. M., Herzberg, O., Moult, J., Herklotz, A., Reinach, F. C., and Smillie, L.B. (1992) Biochemistry 31, 6545-6553). Comparison of the far- and near-UV CD spectra (±Ca2+) of F29W and F29W/ NHdel and titration of the Ca2+-induced ellipticity and fluorescence changes indicates that the deletion has little effect on the global fold of the molecule but reduces the Ca2+ affinity of the N domain, but not the C domain, by 1.6-1.8-fold. Comparisons of the mutants NHdel, F29W, and F29W/NHdel with rTnC have been made using several functional assays. In reconstituted troponin-tropomyosin actomyosin subfragment 1 and myofibrillar ATPase systems, both F29W and NHdel have significantly reduced Ca2+-activated enzymic activities. These effects are cumulative in the double mutant F29W/ NHdel. On the other hand, maximal isometric tension development in Ca2+-activated reconstituted skinned fibers is not affected with F29W and NHdel, although the Ca2+ sensitivity of NHdel in this system is markedly reduced. We conclude that both mutations, NHdel and F29W, are functionally deleterious, possibly affecting interactions of the N domain with troponin I and/or T.

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We investigate electrical properties of InAs/InP semiconductor nanostructures by conductive atomic force microscopy (C-AFM) and current measurements at low temperatures in processed devices. Different conductances and threshold voltages for current onset were observed for each type of nanostructure. In particular, the extremity of the wire could be compared to a dot with similar dimensions. The processed devices were used in order to access the in-plane conductance of an assembly of a reduced number of nanostructures. Here, fluctuations on I-V curves at low temperatures (<40 K) were observed. At these low temperatures and for a suitable range of applied voltages, random telegraph noise (RTN) in the current was observed for devices with dots. These fluctuations can be associated to electrons trapped in dots, as suggested by numerical simulations. A crossover from a semiconductor-like to a metallic transport behavior is also observed for similar parameters. © 2006 WILEY-VCH Verlag GmbH & Co. KGaA.

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Faunal impoverishment and distorted species compositions are common phenomena in oceanic islands; however, many land-bridge islands are poorly inventoried, especially in the Neotropics. We sampled a small mammal community on a land-bridge island (Anchieta Island) along the Brazilian coast. We found only one marsupial Didelphis aurita (Wied-Neuwied, 1826) and two rodent species Oligoryzomys nigripes (Olfers, 1818) and Trinomys iheringi (Thomas, 1911) during 12 months of live trapping and 9195 trap-nights. The diversity of rodents and marsupials was not explained by species-area relations, indicating possible past extinctions. The abundance of D. aurita and O. nigripes was approximately three times higher, while the abundance of T. iheringi was approximately four times lower than abundances reported from other Brazilian Atlantic Forest sites. The population of D. aurita exhibited many phenotypic changes; males were on average 8 % smaller and females produced 30 % less litters than those from the mainland and other land-bridge islands. The long history of forest disturbance, habitat loss, reduction in forest productivity, and the recent introduction of mesopredators may be the major drivers that explain the small mammal community composition on this island. © 2013 Walter de Gruyter GmbH, Berlin/Boston.

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Cellulose micro and nano fibrils were extracted from banana macro fibres and chemically modified using sodium hydroxide, formic acid, 3-methacryloxy propyltrimethoxy silane. These untreated and chemically treated fibrils were incorporated into PF resin and the specimens were prepared. The composites were subjected to long-term water ageing, thermal ageing soil burial and outdoor weathering. The mechanical properties are reduced under all ageing conditions. The present study investigates the effects of different types of ageing on macro fibre, microfibril and nanofibril reinforced PF composites. The effect of chemical modifications of fibres on the degradability of the composites at different environments also has been analysed. © 2013 Elsevier B.V.

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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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Includes bibliography

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Includes bibliography