Анализ влияния физико-химических методов воздействия на продуктивные пласты Ямбургского нефтегазоконденсатного месторождения (ЯНАО)

Во введении раскрывается актуальность выбранной темы, цель и задачи выпускной квалификационной работы. В первой главе изложены теоретические основы методов воздействия, список методов, способы и технологии их проведения и влияние на пласт. Во второй главе дана характеристика изучаемого месторождения. Описана нефтегазоносность месторождения, характеристика коллектора и добываемого газа. В третьей главе проанализированы методы воздействия, применяемые на пласт на ЯНГКМ. В четвертой главе представлен анализ стоимости проведения ГРП. В пятой главе проведен анализ влияния вредных факторов и методы их избежания.The introduction reveals the relevance of the selected topic, the purpose and objectives of the final qualification work. The first chapter sets out the theoretical foundations of impact methods, methods and technologies for their implementation and the effect on the formation. The second chapter describes the studied field. The oil and gas content of the field, the characteristics of the reservoir and produced gas are described. The third chapter analyzes the methods of action applied to the reservoir. The fourth chapter presents an analysis of the cost of hydraulic fracturing. The fifth chapter analyzes the influence of harmful factors and methods of avoidance

Helicobacter pylori VacA Toxin/Subunit p34: Targeting of an Anion Channel to the Inner Mitochondrial Membrane

The vacuolating toxin VacA, released by Helicobacter pylori, is an important virulence factor in the pathogenesis of gastritis and gastroduodenal ulcers. VacA contains two subunits: The p58 subunit mediates entry into target cells, and the p34 subunit mediates targeting to mitochondria and is essential for toxicity. In this study we found that targeting to mitochondria is dependent on a unique signal sequence of 32 uncharged amino acid residues at the p34 N-terminus. Mitochondrial import of p34 is mediated by the import receptor Tom20 and the import channel of the outer membrane TOM complex, leading to insertion of p34 into the mitochondrial inner membrane. p34 assembles in homo-hexamers of extraordinary high stability. CD spectra of the purified protein indicate a content of >40% β-strands, similar to pore-forming β-barrel proteins. p34 forms an anion channel with a conductivity of about 12 pS in 1.5 M KCl buffer. Oligomerization and channel formation are independent both of the 32 uncharged N-terminal residues and of the p58 subunit of the toxin. The conductivity is efficiently blocked by 5-nitro-2-(3-phenylpropylamino)benzoic acid (NPPB), a reagent known to inhibit VacA-mediated apoptosis. We conclude that p34 essentially acts as a small pore-forming toxin, targeted to the mitochondrial inner membrane by a special hydrophobic N-terminal signal

Routinely collected data for randomized trials: promises, barriers, and implications

This work was supported by Stiftung Institut für klinische Epidemiologie. The Meta-Research Innovation Center at Stanford University is funded by a grant from the Laura and John Arnold Foundation. The funders had no role in design and conduct of the study; the collection, management, analysis, or interpretation of the data; or the preparation, review, or approval of the manuscript or its submission for publication.Peer reviewedPublisher PD

SimBench—A Benchmark Dataset of Electric Power Systems to Compare Innovative Solutions Based on Power Flow Analysis

Gefördert durch den Publikationsfonds der Universität Kasse