Amplitude analysis of four-body decays using a massively-parallel fitting framework

The GooFit Framework is designed to perform maximum-likelihood fits for arbitrary functions on various parallel back ends, for example a GPU. We present an extension to GooFit which adds the functionality to perform time-dependent amplitude analyses of pseudoscalar mesons decaying into four pseudoscalar final states. Benchmarks of this functionality show a significant performance increase when utilizing a GPU compared to a CPU. Furthermore, this extension is employed to study the sensitivity on the $D^0 - \bar{D}^0$ mixing parameters $x$ and $y$ in a time-dependent amplitude analysis of the decay $D^0 \rightarrow K^+\pi^-\pi^+\pi^-$. Studying a sample of 50 000 events and setting the central values to the world average of $x = (0.49 \pm0.15) \%$ and $y = (0.61 \pm0.08) \%$, the statistical sensitivities of $x$ and $y$ are determined to be $\sigma(x) = 0.019 \%$ and $\sigma(y) = 0.019 \%$.Comment: Proceedings of the 22nd International Conference on Computing in High Energy and Nuclear Physics, CHEP 201

Inverting Time-Dependent Harmonic Oscillator Potential by a Unitary Transformation and a New Class of Exactly Solvable Oscillators

A time-dependent unitary (canonical) transformation is found which maps the Hamiltonian for a harmonic oscillator with time-dependent real mass and real frequency to that of a generalized harmonic oscillator with time-dependent real mass and imaginary frequency. The latter may be reduced to an ordinary harmonic oscillator by means of another unitary (canonical) transformation. A simple analysis of the resulting system leads to the identification of a previously unknown class of exactly solvable time-dependent oscillators. Furthermore, it is shown how one can apply these results to establish a canonical equivalence between some real and imaginary frequency oscillators. In particular it is shown that a harmonic oscillator whose frequency is constant and whose mass grows linearly in time is canonically equivalent with an oscillator whose frequency changes from being real to imaginary and vice versa repeatedly.Comment: 7 pages, 1 figure include

Particle-hole state densities with non-equidistant single-particle levels

The correct use of energy-dependent single-particle level (s.p.l.) densities within particle-hole state densities based on the equidistant spacing model (ESM) is analysed. First, an analytical expression is obtained following the convolution of energy-dependent excited-particle and hole densities. Next, a comparison is made with results of the ESM formula using average s.p.l. densities for the excited particles and holes, respectively. The Fermi-gas model (FGM) s.p.l. densities calculated at the corresponding average excitation energies are used in both cases. The analysis concerns also the density of particle-hole bound states. The pairing correlations are taken into account while the comparison of various effects includes the exact correction for the Pauli exclusion principle. Quantum-mechanical s.p.l. densities and the continuum effect can also match a corresponding FGM formula, suitable for use within the average energy-dependent partial state density in multistep reaction models.Comment: 29 pages, ReVTeX, 11 postscript figures, submitted to Phys.Rev.

Measurement of the inelastic pp cross-section at a centre-of-mass energy of 13TeV

The cross-section for inelastic proton-proton collisions at a centre-of-mass energy of 13TeV is measured with the LHCb detector. The fiducial cross-section for inelastic interactions producing at least one prompt long-lived charged particle with momentum p > 2 GeV/c in the pseudorapidity range 2 < η < 5 is determined to be ϭ acc = 62:2 ± 0:2 ± 2:5mb. The first uncertainty is the intrinsic systematic uncertainty of the measurement, the second is due to the uncertainty on the integrated luminosity. The statistical uncertainty is negligible. Extrapolation to full phase space yields the total inelastic proton-proton cross-section ϭ inel = 75:4 ± 3:0 ± 4:5mb, where the first uncertainty is experimental and the second due to the extrapolation. An updated value of the inelastic cross-section at a centre-of-mass energy of 7TeV is also reported

Homochirality in biomineral suprastructures induced by assembly of single-enantiomer amino acids from a nonracemic mixture

© 2019, The Author(s). Since Pasteur first successfully separated right-handed and left-handed tartrate crystals in 1848, the understanding of how homochirality is achieved from enantiomeric mixtures has long been incomplete. Here, we report on a chirality dominance effect where organized, three-dimensional homochiral suprastructures of the biomineral calcium carbonate (vaterite) can be induced from a mixed nonracemic amino acid system. Right-handed (counterclockwise) homochiral vaterite helicoids are induced when the amino acid l-Asp is in the majority, whereas left-handed (clockwise) homochiral morphology is induced when d-Asp is in the majority. Unexpectedly, the Asp that incorporates into the homochiral vaterite helicoids maintains the same enantiomer ratio as that of the initial growth solution, thus showing chirality transfer without chirality amplification. Changes in the degree of chirality of the vaterite helicoids are postulated to result from the extent of majority enantiomer assembly on the mineral surface. These mechanistic insights potentially have major implications for high-level advanced materials synthesis

Phosphoinositide-binding interface proteins involved in shaping cell membranes

The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, which contain membrane-deforming domains such as the BAR, EFC/F-BAR, and the IMD/I-BAR domains, led to inward-invaginated tubes or outward protrusions of the membrane, resulting in a variety of membrane shapes. Furthermore, these proteins not only bind to phosphoinositide, but also to the N-WASP/WAVE complex and the actin polymerization machinery, which generates a driving force to shape the membranes