666 research outputs found

    Modeling concept drift: A probabilistic graphical model based approach

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    An often used approach for detecting and adapting to concept drift when doing classi cation is to treat the data as i.i.d. and use changes in classi cation accuracy as an indication of concept drift. In this paper, we take a different perspective and propose a framework, based on probabilistic graphical models, that explicitly represents concept drift using latent variables. To ensure effcient inference and learning, we resort to a variational Bayes inference scheme. As a proof of concept, we demonstrate and analyze the proposed framework using synthetic data sets as well as a real fi nancial data set from a Spanish bank

    Overexpression, crystallization and preliminary X-­ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1

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    The C-terminal cytosolic domain of mouse anoctamin 1 (mANO1, also known as TMEM16A) was cloned, overexpressed, purified and crystallized. The crystals belonged to space group P212121 and diffracted to 2.3 Å resolution

    Search for Lorentz and CPT Violation Effects in Muon Spin Precession

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    The spin precession frequency of muons stored in the (g−2)(g-2) storage ring has been analyzed for evidence of Lorentz and CPT violation. Two Lorentz and CPT violation signatures were searched for: a nonzero Δωa\Delta\omega_{a} (=ωaμ+−ωaμ−\omega_{a}^{\mu^{+}}-\omega_{a}^{\mu^{-}}); and a sidereal variation of ωaμ±\omega_{a}^{\mu^{\pm}}. No significant effect is found, and the following limits on the standard-model extension parameters are obtained: bZ=−(1.0±1.1)×10−23b_{Z} =-(1.0 \pm 1.1)\times 10^{-23} GeV; (mμdZ0+HXY)=(1.8±6.0×10−23)(m_{\mu}d_{Z0}+H_{XY}) = (1.8 \pm 6.0 \times 10^{-23}) GeV; and the 95% confidence level limits bˇ⊥μ+<1.4×10−24\check{b}_{\perp}^{\mu^{+}}< 1.4 \times 10^{-24} GeV and bˇ⊥μ−<2.6×10−24\check{b}_{\perp}^{\mu^{-}} < 2.6 \times 10^{-24} GeV.Comment: 5 pages, 3 figures, submitted to Physical Review Letters, Modified to answer the referees suggestion

    An Improved Limit on the Muon Electric Dipole Moment

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    Three independent searches for an electric dipole moment (EDM) of the positive and negative muons have been performed, using spin precession data from the muon g-2 storage ring at Brookhaven National Laboratory. Details on the experimental apparatus and the three analyses are presented. Since the individual results on the positive and negative muon, as well as the combined result, d=-0.1(0.9)E-19 e-cm, are all consistent with zero, we set a new muon EDM limit, |d| < 1.9E-19 e-cm (95% C.L.). This represents a factor of 5 improvement over the previous best limit on the muon EDM.Comment: 19 pages, 15 figures, 7 table

    Improved Measurement of the Positive Muon Anomalous Magnetic Moment

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    A new measurement of the positive muon's anomalous magnetic moment has been made at the Brookhaven Alternating Gradient Synchrotron using the direct injection of polarized muons into the superferric storage ring. The angular frequency difference omega_{a} between the angular spin precession frequency omega_{s} and the angular orbital frequency omega_{c} is measured as well as the free proton NMR frequency omega_{p}. These determine R = omega_{a} / omega_{p} = 3.707~201(19) times 10^{-3}. With mu_{mu} / mu_{p} = 3.183~345~39(10) this gives a_{mu^+} = 11~659~191(59) times 10^{-10} (pm 5 ppm), in good agreement with the previous CERN and BNL measurements for mu^+ and mu^-, and with the standard model prediction.Comment: 4 pages, 4 figures. accepted for publication in Phys. Rev. D62 Rapid Communication

    Search for Lorentz and CPT Violation Effects in Muon Spin Precession

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    The spin precession frequency of muons stored in the (g−2)(g-2) storage ring has been analyzed for evidence of Lorentz and CPT violation. Two Lorentz and CPT violation signatures were searched for: a nonzero Δωa\Delta\omega_{a} (=ωaμ+−ωaμ−\omega_{a}^{\mu^{+}}-\omega_{a}^{\mu^{-}}); and a sidereal variation of ωaμ±\omega_{a}^{\mu^{\pm}}. No significant effect is found, and the following limits on the standard-model extension parameters are obtained: bZ=−(1.0±1.1)×10−23b_{Z} =-(1.0 \pm 1.1)\times 10^{-23} GeV; (mμdZ0+HXY)=(1.8±6.0×10−23)(m_{\mu}d_{Z0}+H_{XY}) = (1.8 \pm 6.0 \times 10^{-23}) GeV; and the 95% confidence level limits bˇ⊥μ+<1.4×10−24\check{b}_{\perp}^{\mu^{+}}< 1.4 \times 10^{-24} GeV and bˇ⊥μ−<2.6×10−24\check{b}_{\perp}^{\mu^{-}} < 2.6 \times 10^{-24} GeV.Comment: 5 pages, 3 figures, submitted to Physical Review Letters, Modified to answer the referees suggestion

    The structure of the complex between a-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism

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    Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). Whereas tubulin heterodimer formation is well-characterized biochemically, its dissociation pathway is not clearly understood. Here, we carried out biochemical assays to dissect the role of the human TBCE and TBCB chaperones in a-tubulin–b-tubulin dissociation. We used electron microscopy and image processing to determine the three-dimensional structure of the human TBCE, TBCB and a-tubulin (aEB) complex, which is formed upon a-tubulin–b-tubulin heterodimer dissociation by the two chaperones. Docking the atomic structures of domains of these proteins, including the TBCE UBL domain, as we determined by X-ray crystallography, allowed description of the molecular architecture of the aEB complex. We found that heterodimer dissociation is an energy-independent process that takes place through a disruption of the a-tubulin–b-tubulin interface that is caused by a steric interaction between b-tubulin and the TBCE cytoskeleton-associated protein glycine-rich (CAP-Gly) and leucine-rich repeat (LRR) domains. The protruding arrangement of chaperone ubiquitin-like (UBL) domains in the aEB complex suggests that there is a direct interaction of this complex with the proteasome, thus mediating a-tubulin degradation

    Final Report of the Muon E821 Anomalous Magnetic Moment Measurement at BNL

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    We present the final report from a series of precision measurements of the muon anomalous magnetic moment, a_mu = (g-2)/2. The details of the experimental method, apparatus, data taking, and analysis are summarized. Data obtained at Brookhaven National Laboratory, using nearly equal samples of positive and negative muons, were used to deduce a_mu(Expt) = 11 659 208.0(5.4)(3.3) x 10^-10, where the statistical and systematic uncertainties are given, respectively. The combined uncertainty of 0.54 ppm represents a 14-fold improvement compared to previous measurements at CERN. The standard model value for a_mu includes contributions from virtual QED, weak, and hadronic processes. While the QED processes account for most of the anomaly, the largest theoretical uncertainty, ~0.55 ppm, is associated with first-order hadronic vacuum polarization. Present standard model evaluations, based on e+e- hadronic cross sections, lie 2.2 - 2.7 standard deviations below the experimental result.Comment: Summary paper of E821 Collaboration measurements of the muon anomalous magnetic moment, each reported earlier in Letters or Brief Reports; 96 pages, 41 figures, 16 tables. Revised version submitted to PR

    Planet Populations as a Function of Stellar Properties

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    Exoplanets around different types of stars provide a window into the diverse environments in which planets form. This chapter describes the observed relations between exoplanet populations and stellar properties and how they connect to planet formation in protoplanetary disks. Giant planets occur more frequently around more metal-rich and more massive stars. These findings support the core accretion theory of planet formation, in which the cores of giant planets form more rapidly in more metal-rich and more massive protoplanetary disks. Smaller planets, those with sizes roughly between Earth and Neptune, exhibit different scaling relations with stellar properties. These planets are found around stars with a wide range of metallicities and occur more frequently around lower mass stars. This indicates that planet formation takes place in a wide range of environments, yet it is not clear why planets form more efficiently around low mass stars. Going forward, exoplanet surveys targeting M dwarfs will characterize the exoplanet population around the lowest mass stars. In combination with ongoing stellar characterization, this will help us understand the formation of planets in a large range of environments.Comment: Accepted for Publication in the Handbook of Exoplanet

    Structure Analysis of a New Psychrophilic Marine Protease

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    A new psychrophilic marine protease was found from a marine bacterium Flavobacterium YS-80 in the Chinese Yellow Sea. The protease is about 49 kD with an isoelectric point about 4.5. It consists of 480 amino acids and is homologous to a psychrophilic alkaline protease (PAP) from an Antarctic Pseudomonas species. The protein was purified from the natural bacterium fermented and crystallized. Its crystal structure (PDB ID 3U1R) was solved at 2.0 Å by Molecular Replacement using a model based on PAP, and was refined to a crystallographic Rwork of 0.16 and an Rfree of 0.21. The marine protease consists of a two domain structure with an N-terminal domain including residues 37–264 and a C-terminal domain including residues 265–480. Similar to PAP, the N-terminal domain is responsible for proteolysis and the C-terminal is for stability. His186, His190, His196 and Tyr226 are ligands for the Zn2+ ion in the catalytic center. The enzyme's Tyr226 is closer to the Zn2+ ion than in PAP and it shows a stronger Zn2+―Tyr-OH bond. There are eight calcium ions in the marine protease molecule and they have significantly shorter bond distances to their ligands compared to their counterparts in all three crystal forms of PAP. On the other hand, the loops in the marine protease are more compact than in PAP. This makes the total structure stable and less flexible, resulting in higher thermo stability. These properties are consistent with the respective environments of the proteases. The structural analysis of this new marine protease provides new information for the study of psychrophilic proteases and is helpful for elucidating the structure-environment adaptation of these enzymes
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