Construção de modelos de interação in silico e in vitro do inibidor do tipo Kunitz de Adenanthera pavonina L. para as enzimas cisteínicas e serínicas

Serines proteinases inhibitors (PIs) are widely distributed in nature and are able to inhibit both in vitro and in vivo enzymatic activites. Seed PIs in than leguminous are classified in seven families, Bowman-Birk and Kunitz type families that most studied representing an important role in the first line of defense toward insects pests. Some Kunitz type inhibitors possess activities serine and cysteine for proteinases named bifunctional inhibitor, as ApTKI the inhibitor isolate from seed of Adenanthera pavonina. The A. pavonina inhibitor presenting the uncommon property and was used for interaction studies between proteinases serine (trypsin) and cysteine (papain). In order to determinate the in vitro interaction of ApTKI against enzymes inhibitor purification was carried cut by using chromatographic techniques and inhibition assays. The 3D model of the bifunctional inhibitor ApTKI was constructed SWISS-MODEL program by homology modeling using soybean trypsin inhibitor (STI, pdb:1ba7), as template which presented 40% of identity to A. pavonina inhibitor. Model quality was evaluated by PROCHECK program. Moreover in silico analyzes of formed complex between the enzymes and ApTKI was evaluated by HEX 4.5 program. In vitro results confirmed the inhibitory assays, where the inhibitor presented the ability to simultaneously inhibit trypsin and papain. The residues encountered in the inhibitor model of folder structural three-dimensional that make contact to enzymes target coud explain the specificity pattern against serine and cysteine proteinases

Uma fonte chaveada de 50kW com correção de fator de potência para alimentação de uma tocha de plasma Indutiva utilizando técnicas de controle digital

This work deals with the development of an experimental study on a power supply of high frequency that provides the toch plasmica to be implemented in PLASPETRO project, which consists of two static converters developed by using Insulated Gate Bipolar Transistor (IGBT). The drivers used to control these keys are triggered by Digital Signal Processor (DSP) through optical fibers to reduce problems with electromagnetic interference (EMI). The first stage consists of a pre-regulator in the form of an AC to DC converter with three-phase boost power factor correction which is the main theme of this work, while the second is the source of high frequency itself. A series-resonant inverter consists of four (4) cell inverters operating in a frequency around 115 kHz each one in soft switching mode, alternating itself to supply the load (plasma torch) an alternating current with a frequency of 450 kHz. The first stage has the function of providing the series-resonant inverter a DC voltage, with the value controlled from the power supply provided by the electrical system of the utility, and correct the power factor of the system as a whole. This level of DC bus voltage at the output of the first stage will be used to control the power transferred by the inverter to the load, and it may vary from 550 VDC to a maximum of 800 VDC. To control the voltage level of DC bus driver used a proportional integral (PI) controller and to achieve the unity power factor it was used two other proportional integral currents controllers. Computational simulations were performed to assist in sizing and forecasting performance. All the control and communications needed to stage supervisory were implemented on a DSP

Controle em modo dual adaptativo robusto aplicado a um sistema de geração de energia elétrica

Synchronous machines, widely used in energy generation systems, require constant voltage and frequency to obtain good quality of energy. However, for large load variati- ons, it is difficult to maintain outputs on nominal values due to parametric uncertainties, nonlinearities and coupling among variables. Then, we propose to apply the Dual Mode Adaptive Robust Controller (DMARC) in the field flux control loop, replacing the tradi- tional PI controller. The DMARC links a Model Reference Adaptive Controller (MRAC) and a Variable Structure Model Reference Adaptive Controller (VS-MRAC), incorpora- ting transient performance advantages from VS-MRAC and steady state properties from MRAC. Moreover, simulation results are included to corroborate the theoretical studies.

Construção de modelos de interação in silico e in vitro do inibidor do tipo Kunitz de Adenanthera pavonina L. para as enzimas cisteínicas e serínicas

Serines proteinases inhibitors (PIs) are widely distributed in nature and are able to inhibit both in vitro and in vivo enzymatic activites. Seed PIs in than leguminous are classified in seven families, Bowman-Birk and Kunitz type families that most studied representing an important role in the first line of defense toward insects pests. Some Kunitz type inhibitors possess activities serine and cysteine for proteinases named bifunctional inhibitor, as ApTKI the inhibitor isolate from seed of Adenanthera pavonina. The A. pavonina inhibitor presenting the uncommon property and was used for interaction studies between proteinases serine (trypsin) and cysteine (papain). In order to determinate the in vitro interaction of ApTKI against enzymes inhibitor purification was carried cut by using chromatographic techniques and inhibition assays. The 3D model of the bifunctional inhibitor ApTKI was constructed SWISS-MODEL program by homology modeling using soybean trypsin inhibitor (STI, pdb:1ba7), as template which presented 40% of identity to A. pavonina inhibitor. Model quality was evaluated by PROCHECK program. Moreover in silico analyzes of formed complex between the enzymes and ApTKI was evaluated by HEX 4.5 program. In vitro results confirmed the inhibitory assays, where the inhibitor presented the ability to simultaneously inhibit trypsin and papain. The residues encountered in the inhibitor model of folder structural three-dimensional that make contact to enzymes target coud explain the specificity pattern against serine and cysteine proteinases