2,022 research outputs found

    Energy gap measurement of nanostructured thin aluminium films for use in single Cooper-pair devices

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    Within the context of superconducting gap engineering, Al-\alox-Al tunnel junctions have been used to study the variation in superconducting gap, Δ\Delta, with film thickness. Films of thickness 5, 7, 10 and 30 nm were used to form the small area superconductor-insulator-superconductor (SIS) tunnel junctions. In agreement with previous measurements we have observed an increase in the superconducting energy gap of aluminium with a decrease in film thickness. In addition, we find grain size in small area films with thickness \textbf{\geq} 10 nm has no appreciable effect on energy gap. Finally, we utilize 7 and 30 nm films in a single Cooper-pair transistor, and observe the modification of the finite bias transport processes due to the engineered gap profile

    Test Methods for Image-Based Information in Next-Generation Manufacturing

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    Typical control designs in the process systems engineering literature have assumed that the primary sensing methodologies are traditional instruments such as thermocouples. Dig- italization is changing the landscape for manufacturing, and data-based sensing modalities (e.g., image-based sensing) are becoming of greater interest for plant control. These considerations require novel test/evaluation solutions. For example, process systems engineering researchers may wish to test image-based sensors in simulation. In this work, we provide preliminary thoughts on how image-based technologies might be evaluated via simulation for process systems

    Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

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    Poly(ADP-ribose) polymerase 1 (PARP1) synthesizes poly(ADP-ribose) (PAR) using nicotinamide adenine dinucleotide (NAD) as a substrate. Despite intensive research on the cellular functions of PARP1, the molecular mechanism of PAR formation has not been comprehensively understood. In this study, we elucidate the molecular mechanisms of poly(ADP-ribosyl)ation and identify PAR acceptor sites. Generation of different chimera proteins revealed that the amino-terminal domains of PARP1, PARP2 and PARP3 cooperate tightly with their corresponding catalytic domains. The DNA-dependent interaction between the amino-terminal DNA-binding domain and the catalytic domain of PARP1 increased Vmax and decreased the Km for NAD. Furthermore, we show that glutamic acid residues in the auto-modification domain of PARP1 are not required for PAR formation. Instead, we identify individual lysine residues as acceptor sites for ADP-ribosylation. Together, our findings provide novel mechanistic insights into PAR synthesis with significant relevance for the different biological functions of PARP family members
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