A Radiation-Hard Dual Channel 4-bit Pipeline for a 12-bit 40 MS/s ADC Prototype with extended Dynamic Range for the ATLAS Liquid Argon Calorimeter Readout Electronics Upgrade at the CERN LHC

The design of a radiation-hard dual channel 12-bit 40 MS/s pipeline ADC with extended dynamic range is presented, for use in the readout electronics upgrade for the ATLAS Liquid Argon Calorimeters at the CERN Large Hadron Collider. The design consists of two pipeline A/D channels with four Multiplying Digital-to-Analog Converters with nominal 12-bit resolution each. The design, fabricated in the IBM 130 nm CMOS process, shows a performance of 68 dB SNDR at 18 MHz for a single channel at 40 MS/s while consuming 55 mW/channel from a 2.5 V supply, and exhibits no performance degradation after irradiation. Various gain selection algorithms to achieve the extended dynamic range are implemented and tested.Comment: 22 pages, 22 figures, accepted by JINS

A radiation-hard dual-channel 12-bit 40 MS/s ADC prototype for the ATLAS liquid argon calorimeter readout electronics upgrade at the CERN LHC

The readout electronics upgrade for the ATLAS Liquid Argon Calorimeters at the CERN Large Hadron Collider requires a radiation-hard ADC. The design of a radiation-hard dual-channel 12-bit 40 MS/s pipeline ADC for this use is presented. The design consists of two pipeline A/D channels each with four Multiplying Digital-to-Analog Converters followed by 8-bit Successive-Approximation-Register analog-to-digital converters. The custom design, fabricated in a commercial 130 nm CMOS process, shows a performance of 67.9 dB SNDR at 10 MHz for a single channel at 40 MS/s, with a latency of 87.5 ns (to first bit read out), while its total power consumption is 50 mW/channel. The chip uses two power supply voltages: 1.2 and 2.5 V. The sensitivity to single event effects during irradiation is measured and determined to meet the system requirements

Elastic properties of ribosomal RNA building blocks: molecular dynamics of the GTPase-associated center rRNA

Explicit solvent molecular dynamics (MD) was used to describe the intrinsic flexibility of the helix 42–44 portion of the 23S rRNA (abbreviated as Kt-42+rGAC; kink-turn 42 and GTPase-associated center rRNA). The bottom part of this molecule consists of alternating rigid and flexible segments. The first flexible segment (Hinge1) is the highly anharmonic kink of Kt-42. The second one (Hinge2) is localized at the junction between helix 42 and helices 43/44. The rigid segments are the two arms of helix 42 flanking the kink. The whole molecule ends up with compact helices 43/44 (Head) which appear to be modestly compressed towards the subunit in the Haloarcula marismortui X-ray structure. Overall, the helix 42–44 rRNA is constructed as a sophisticated intrinsically flexible anisotropic molecular limb. The leading flexibility modes include bending at the hinges and twisting. The Head shows visible internal conformational plasticity, stemming from an intricate set of base pairing patterns including dynamical triads and tetrads. In summary, we demonstrate how rRNA building blocks with contrasting intrinsic flexibilities can form larger architectures with highly specific patterns of preferred low-energy motions and geometries

Conformations of Flanking Bases in HIV-1 RNA DIS Kissing Complexes Studied by Molecular Dynamics

Explicit solvent molecular dynamics simulations (in total almost 800 ns including locally enhanced sampling runs) were applied with different ion conditions and with two force fields (AMBER and CHARMM) to characterize typical geometries adopted by the flanking bases in the RNA kissing-loop complexes. We focus on flanking base positions in multiple x-ray and NMR structures of HIV-1 DIS kissing complexes and kissing complex from the large ribosomal subunit of Haloarcula marismortui. An initial x-ray open conformation of bulged-out bases in HIV-1 DIS complexes, affected by crystal packing, tends to convert to a closed conformation formed by consecutive stretch of four stacked purine bases. This is in agreement with those recent crystals where the packing is essentially avoided. We also observed variants of the closed conformation with three stacked bases, while nonnegligible populations of stacked geometries with bulged-in bases were detected, too. The simulation results reconcile differences in positions of the flanking bases observed in x-ray and NMR studies. Our results suggest that bulged-out geometries are somewhat more preferred, which is in accord with recent experiments showing that they may mediate tertiary contacts in biomolecular assemblies or allow binding of aminoglycoside antibiotics

Where Brain, Body and World Collide

The production cross section of electrons from semileptonic decays of beauty hadrons was measured at mid-rapidity (|y| < 0.8) in the transverse momentum range 1 < pt < 8 Gev/c with the ALICE experiment at the CERN LHC in pp collisions at a center of mass energy sqrt{s} = 7 TeV using an integrated luminosity of 2.2 nb^{-1}. Electrons from beauty hadron decays were selected based on the displacement of the decay vertex from the collision vertex. A perturbative QCD calculation agrees with the measurement within uncertainties. The data were extrapolated to the full phase space to determine the total cross section for the production of beauty quark-antiquark pairs

Hinge-Like Motions in RNA Kink-Turns: The Role of the Second A-Minor Motif and Nominally Unpaired Bases

Kink-turn (K-turn) motifs are asymmetric internal loops found at conserved positions in diverse RNAs, with sharp bends in phosphodiester backbones producing V-shaped structures. Explicit-solvent molecular dynamics simulations were carried out for three K-turns from 23S rRNA, i.e., Kt-38 located at the base of the A-site finger, Kt-42 located at the base of the L7/L12 stalk, and Kt-58 located in domain III, and for the K-turn of human U4 snRNA. The simulations reveal hinge-like K-turn motions on the nanosecond timescale. The first conserved A-minor interaction between the K-turn stems is entirely stable in all simulations. The angle between the helical arms of Kt-38 and Kt-42 is regulated by local variations of the second A-minor (type I) interaction between the stems. Its variability ranges from closed geometries to open ones stabilized by insertion of long-residency waters between adenine and cytosine. The simulated A-minor geometries fully agree with x-ray data. Kt-58 and Kt-U4 exhibit similar elbow-like motions caused by conformational change of the adenosine from the nominally unpaired region. Despite the observed substantial dynamics of K-turns, key tertiary interactions are stable and no sign of unfolding is seen. We suggest that some K-turns are flexible elements mediating large-scale ribosomal motions during the protein synthesis cycle