Thermocouple simulator

NERMUT, M. Termočlánkový simulátor. Brno: Vysoké učení technické v Brně, Fakulta elektrotechniky a komunikačních technologií, 2009. 62 s. Pedagogický vedoucí bakalářské práce Ing. Stanislav Klusáček. Konzultant Ing. Miroslav Krupa, - IDC Brno, Honeywell s.r.o. Cílem práce je návrh a konstrukce příručního termočlánkového simulátoru, vhodného do laboratoře i do provozu. Přístroj lze ovládat ručně nebo linkou RS232. Důraz je kladen na všestrannost přístroje, snadné ovládání, bezpečný provoz (galvanické oddělení), řádně provedenou teplotní kompenzaci studeného konce, snadnou kalibraci nelinearity. Zadavatelem práce je IDC Honeywell Brno. Základní prameny: - Katalog firmy OMEGA (Temperature Handbook) - Manuály přístrojů OMEGA (www.omega.com) - Katalogové listy termočlánkových simulátorů jiných výrobců (zdroj: internet) - Isotech Traceable Book – Temperature Calibrabration (www.isotech.co.uk) - BELZA J., Nabíječka Li-ion článků (www.belza.cz) Přílohy: - Návod k použití realizovaného přístroj - Elektrické schéma - Kalibrační data - CD (zdrojový kód)NERMUT, M. Thermocouple simulator. Brno: Brno University of Technology, Faculty of Eletrical Engineering and Communication. 2009. 62 s. Supervisor Ing. Stanislav Klusáček. Consultant Ing. Miroslav Krupa, - IDC Brno, Honeywell s.r.o. The aim of the thesis is design and realization of handheld thermocouple simulator, suitable both for laboratory and plant use. Manual or remote control via RS232 are possible. Special attention is focused on universality, easy and safety use (galvanic isolation), properly cold junction compensation, easy calibration of non-linearity. Sponsor: IDC Honeywell, Brno, Czech Republic Basic literature: - OMEGA Temperature Handbook) - Datasheets of OMEGA instruments (www.omega.com) - Datasheets of other vendor instruments (www) - Isotech Traceable Book – Temperature Calibrabration (www.isotech.co.uk) - BELZA J., Buld-in Li-ion accu charger (www.belza.cz) Appendixs: - User manual - Schematic - Calibration data - CD (source code)

HIV-1 Protease and Reverse Transcriptase Control the Architecture of Their Nucleocapsid Partner

The HIV-1 nucleocapsid is formed during protease (PR)-directed viral maturation, and is transformed into pre-integration complexes following reverse transcription in the cytoplasm of the infected cell. Here, we report a detailed transmission electron microscopy analysis of the impact of HIV-1 PR and reverse transcriptase (RT) on nucleocapsid plasticity, using in vitro reconstitutions. After binding to nucleic acids, NCp15, a proteolytic intermediate of nucleocapsid protein (NC), was processed at its C-terminus by PR, yielding premature NC (NCp9) followed by mature NC (NCp7), through the consecutive removal of p6 and p1. This allowed NC co-aggregation with its single-stranded nucleic-acid substrate. Examination of these co-aggregates for the ability of RT to catalyse reverse transcription showed an effective synthesis of double-stranded DNA that, remarkably, escaped from the aggregates more efficiently with NCp7 than with NCp9. These data offer a compelling explanation for results from previous virological studies that focused on i) Gag processing leading to nucleocapsid condensation, and ii) the disappearance of NCp7 from the HIV-1 pre-integration complexes. We propose that HIV-1 PR and RT, by controlling the nucleocapsid architecture during the steps of condensation and dismantling, engage in a successive nucleoprotein-remodelling process that spatiotemporally coordinates the pre-integration steps of HIV-1. Finally we suggest that nucleoprotein remodelling mechanisms are common features developed by mobile genetic elements to ensure successful replication

Publicly funded bariatric surgery in Australia. What guidance is provided by the States and Territories?

Publicly funded bariatric surgery in Australia. What guidance is provided by the States and Territories

Control of human immunodeficiency virus type-1 protease activity in insect cells expressing Gag-Pol rescues assembly of immature but not mature virus-like particles

Expression of human immunodeficiency virus type 1 (HIV-1) Gag protein in insect cells using baculovirus vectors leads to the abundant production of virus-like particles (VLPs) that represent the immature form of the virus. When Gag-Pol is included, however, VLP production is abolished, a result attributed to premature protease activation degrading the intracellular pool of Gag precursor before particle assembly can occur. As large-scale synthesis of mature noninfectious VLPs would be useful, we have sought to control HIV protease activity in insect cells to give a balance of Gag and Gag-Pol that is compatible with mature particle formation. We show here that intermediate levels of protease activity in insect cells can be attained through site-directed mutagenesis of the protease and through antiprotease drug treatment. However, despite Gag cleavage patterns that mimicked those seen in mammalian cells, VLP synthesis exhibited an essentially all-or-none response in which VLP synthesis occurred but was immature or failed completely. Our data are consistent with a requirement for specific cellular factors in addition to the correct ratio of Gag and Gag-Pol for assembly of mature retrovirus particles in heterologous cell types. (C) 2003 Elsevier Science (USA). All rights reserved