Measurements of atmospheric neutrinos and antineutrinos in the MINOS far detector

This paper reports measurements of atmospheric neutrino and antineutrino interactions in the MINOS Far Detector, based on 2553 live-days (37.9 kton-years) of data. A total of 2072 candidate events are observed. These are separated into 905 contained-vertex muons and 466 neutrino-induced rock-muons, both produced by charged-current v_µ and v¯_µ interactions, and 701 contained-vertex showers, composed mainly of charged-current v_e and v¯_e interactions and neutral-current interactions. The curvature of muon tracks in the magnetic field of the MINOS Far Detector is used to select separate samples of v_µ and v¯_µ events. The observed ration of v¯_µ to v_µ events is compared with the Monte Carlo (MC) simulation, giving a double ration of (R^(data)_(v¯/v))/(R^(MC)_(v¯/v)) = 1.03 ± 0.08(stat) ± 0.08(syst). The v_µ and v¯_µ data are separated into bins of L/E resolution, based on the reconstructed energy and direction of each event, and a maximum likelihood fit to the observed L/E distributions is used to determine the atmospheric neutrino oscillation parameters. This fit returns 90% confidence limits of |Δm^2| = (1.9 ± 0.4) x 10^(-3) eV^2 and sin^(2)2θ > 0.86. The fit is extended to incorporate separate v_µ and v¯_µ oscillation parameters, returning 90% confidence limits of |Δm^2|-|Δm¯^2| = 0.6^(2.4)_(-0.8) x 10^(-3) eV^2 on the difference between the squared-mass splittings for neutrinos and antineutrinos

Understanding protein non-folding

This review describes the family of intrinsically disordered proteins, members of which fail to form rigid 3-D structures under physiological conditions, either along their entire lengths or only in localized regions. Instead, these intriguing proteins/regions exist as dynamic ensembles within which atom positions and backbone Ramachandran angles exhibit extreme temporal fluctuations without specific equilibrium values. Many of these intrinsically disordered proteins are known to carry out important biological functions which, in fact, depend on the absence of specific 3-D structure. The existence of such proteins does not fit the prevailing structure-function paradigm, which states that unique 3-D structure is a prerequisite to function. Thus, the protein structure-function paradigm has to be expanded to include intrinsically disordered proteins and alternative relationships among protein sequence, structure, and function. This shift in the paradigm represents a major breakthrough for biochemistry, biophysics and molecular biology, as it opens new levels of understanding with regard to the complex life of proteins. This review will try to answer the following questions: How were intrinsically disordered proteins discovered? Why don't these proteins fold? What is so special about intrinsic disorder? What are the functional advantages of disordered proteins/regions? What is the functional repertoire of these proteins? What are the relationships between intrinsically disordered proteins and human diseases

Construction of precision wire readout planes for the Short-Baseline Near Detector (SBND)

The Short-Baseline Near Detector time projection chamber is unique in the design of its charge readout planes. These anode plane assemblies (APAs) have been fabricated and assembled to meet strict accuracy and precision requirements: wire spacing of 3 mm +/- 0.5 mm and wire tension of 7 N +/- 1 N across 3,964 wires per APA, and flatness within 0.5 mm over the 4 m +/- 2.5 m extent of each APA. This paper describes the design, manufacture and assembly of these key detector components, with a focus on the quality assurance at each stage