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Schwartz, T.

Publications and source records attributed to Schwartz, T..

The New Small Wheel electronics

The increase in luminosity, and consequent higher backgrounds, of the LHC upgrades require improved rejection of fake tracks in the forward region of the ATLAS Muon Spectrometer. The New Small Wheel upgrade of the Muon Spectrometer aims to reduce the large background of fake triggers from track segments that don't originate from the interaction point. The New Small Wheel employs two detector technologies, the resistive strip Micromegas detectors and the “small” Thin Gap Chambers, with a total of 2.45 million electrodes to be sensed. The two technologies require the design of a complex electronics system given that it consists of two different detector technologies and is required to provide both precision readout and a fast trigger. It will operate in a high background radiation region up to about 20 kHz/cm 2 at the expected HL-LHC luminosity of $\mathcal{L}$= 7.5 × 10 34 cm -2 s -1 . The architecture of the system is strongly defined by the GBTx data aggregation ASIC, the newly-introduced FELIX data router and the software based data handler of the ATLAS detector. The electronics complex of this new detector was designed and developed in the last ten years and consists of multiple radiation tolerant Application Specific Integrated Circuits, multiple front-end boards, dense boards with FPGA's and purpose-built Trigger Processor boards within the ATCA standard. The New Small Wheel has been installed in 2021 and is undergoing integration within ATLAS for LHC Run 3. It should operate through the end of Run 4 (December 2032). In this manuscript, the overall design of the New Small Wheel electronics is presented.

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Proteolytic dissection of Zab, the Z-DNA-binding domain of human ADAR1

Zalpha is a peptide motif that binds to Z-DNA with high affinity. This motif binds to alternating dC-dG sequences stabilized in the Z-conformation by means of bromination or supercoiling, but not to B-DNA. Zalpha is part of the N-terminal region of double-stranded RNA adenosine deaminase (ADAR1), a candidate enzyme for nuclear pre-mRNA editing in mammals. Zalpha is conserved in ADAR1 from many species; in each case, there is a second similar motif, Zbeta, separated from Zalpha by a more divergent linker. To investigate the structure-function relationship of Zalpha, its domain structure was studied by limited proteolysis. Proteolytic profiles indicated that Zalpha is part of a domain, Zab, of 229 amino acids (residues 133-361 in human ADAR1). This domain contains both Zalpha and Zbeta as well as a tandem repeat of a 49-amino acid linker module. Prolonged proteolysis revealed a minimal core domain of 77 amino acids (positions 133-209), containing only Zalpha, which is sufficient to bind left-handed Z-DNA; however, the substrate binding is strikingly different from that of Zab. The second motif, Zbeta, retains its structural integrity only in the context of Zab and does not bind Z-DNA as a separate entity. These results suggest that Zalpha and Zbeta act as a single bipartite domain. In the presence of substrate DNA, Zab becomes more resistant to proteases, suggesting that it adopts a more rigid structure when bound to its substrate, possibly with conformational changes in parts of the protein.

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