Quasi-free Compton Scattering and the Polarizabilities of the Neutron

Differential cross sections for quasi-free Compton scattering from the proton and neutron bound in the deuteron have been measured using the Glasgow/Mainz tagging spectrometer at the Mainz MAMI accelerator together with the Mainz 48 cm $\oslash$ $\times$ 64 cm NaI(Tl) photon detector and the G\"ottingen SENECA recoil detector. The data cover photon energies ranging from 200 MeV to 400 MeV at $\theta^{LAB}_\gamma=136.2^\circ$. Liquid deuterium and hydrogen targets allowed direct comparison of free and quasi-free scattering from the proton. The neutron detection efficiency of the SENECA detector was measured via the reaction $p(\gamma,\pi^+ n)$. The "free" proton Compton scattering cross sections extracted from the bound proton data are in reasonable agreement with those for the free proton which gives confidence in the method to extract the differential cross section for free scattering from quasi-free data. Differential cross sections on the free neutron have been extracted and the difference of the electromagnetic polarizabilities of the neutron have been obtained to be $\alpha-\beta= 9.8\pm 3.6(stat){}^{2.1}_1.1(syst)\pm 2.2(model)$ in units $10^{-4}fm^3$. In combination with the polarizability sum $\alpha +\beta=15.2\pm 0.5$ deduced from photoabsorption data, the neutron electric and magnetic polarizabilities, $\alpha_n=12.5\pm 1.8(stat){}^{+1.1}_{-0.6}\pm 1.1(model)$ and $\beta_n=2.7\mp 1.8(stat){}^{+0.6}_{-1.1}(syst)\mp 1.1(model)$ are obtained. The backward spin polarizability of the neutron was determined to be $\gamma^{(n)}_\pi=(58.6\pm 4.0)\times 10^{-4}fm^4$

Neutron polarizabilities investigated by quasi-free Compton scattering from the deuteron

Measuring Compton scattered photons and recoil neutrons in coincidence, quasi-free Compton scattering by the neutron has been investigated at MAMI (Mainz) at $theta^{lab}_\gamma=136^o$ in an energy range from 200 to 400 MeV. From the data a polarizability difference of $\alpha_n - \beta_n = 9.8 \pm 3.6(stat)^{+2.1}_{-1.1}(syst)\pm 2.2(model)$ in units of $10^{-4}fm^3$ has been determined. In combination with the polarizability sum $\alpha_n+\beta_n= 15.2\pm 0.5$ deduced from photo absorption data, the neutron electric and magnetic polarizabilities, $\alpha_n=12.5\pm 1.8(stat)^{+1.1}_{-0.6}(syst)\pm 1.1(model)$ and $\beta_n = 2.7\mp 1.8(stat)^{+0.6}_{-1.1}(syst)\mp 1.1(model)$, are obtained

Quasi-free π0\pi^0 Photoproduction from the Bound Nucleon

Differential cross-sections for quasi-free $\pi^0$ photoproduction from the proton and neutron bound in the deuteron have been measured for $E_\gamma= 200 - 400$ MeV at $\theta^{\rm lab}_\gamma = 136.2^\circ$ usind the Glasgow photon tagger at MAMI, the Mainz 48 cm $\varnothing$ $\times$ 64 cm NaI(Tl) photon detector and the G\"ottingen SENECA recoil detector. For the proton measurements made with both liquid deuterium and liquid hydrogen targets allow direct comparison of "free" $\pi^0$ photoproduction cross-sections as extracted from the bound proton data with experimental free cross sections which are found to be in reasonable agreement below 320 MeV. At higher energies the "free" cross sections extracted from quasifree data are significantly smaller than the experimental free cross sections and theoretical predictions based on multipole analysis. For the first time, "free" neutron cross sections have been extracted in the $\Delta$-region. They are also in agreement with the predictions from multipole analysis up to 320 MeV and significantly smaller at higher photon energies

Structural determinants of PINK1 topology and dual subcellular distribution

<p>Abstract</p> <p>Background</p> <p>PINK1 is a mitochondria-targeted kinase that constitutively localizes to both the mitochondria and the cytosol. The mechanism of how PINK1 achieves cytosolic localization following mitochondrial processing remains unknown. Understanding PINK1 subcellular localization will give us insights into PINK1 functions and how mutations in PINK1 lead to Parkinson's disease. We asked how the mitochondrial localization signal, the transmembrane domain, and the kinase domain participate in PINK1 localization.</p> <p>Results</p> <p>We confirmed that PINK1 mitochondrial targeting signal is responsible for mitochondrial localization. Once inside the mitochondria, we found that both PINK1 transmembrane and kinase domain are important for membrane tethering and cytosolic-facing topology. We also showed that PINK1 dual subcellular distribution requires both Hsp90 interaction with the kinase domain and the proteolysis at a cleavage site downstream of the transmembrane domain because removal of this cleavage site completely abolished cytosolic PINK1. In addition, the disruption of the Hsp90-PINK1 interaction increased mitochondrial PINK1 level.</p> <p>Conclusion</p> <p>Together, we believe that once PINK1 enters the mitochondria, PINK1 adopts a tethered topology because the transmembrane domain and the kinase domain prevent PINK1 forward movement into the mitochondria. Subsequent proteolysis downstream of the transmembrane domain then releases PINK1 for retrograde movement while PINK1 kinase domain interacts with Hsp90 chaperone. The significance of this dual localization could mean that PINK1 has compartmental-specific functions.</p

The helicity amplitudes A1/2_{1/2} and A3/2_{3/2} for the D13(1520)_{13}(1520) resonance obtained from the γ⃗p⃗→pπ0\vec{\gamma} \vec{p} \to p \pi^0 reaction}

The helicity dependence of the $\vec{\gamma} \vec{p} \to p \pi^0$ reaction has been measured for the first time in the photon energy range from 550 to 790 MeV. The experiment, performed at the Mainz microtron MAMI, used a 4$\pi$-detector system, a circularly polarized, tagged photon beam, and a longitudinally polarized frozen-spin target. These data are predominantly sensitive to the $D_{13}(1520)$ resonance and are used to determine its parameters.Comment: 5 pages, 4 figure

Acer rubrum Wats.

https://thekeep.eiu.edu/herbarium_specimens_byname/21742/thumbnail.jp

First measurement of the Gerasimov-Drell-Hearn integral for Hydrogen from 200 to 800 MeV

A direct measurement of the helicity dependence of the total photoabsorption cross section on the proton was carried out at MAMI (Mainz) in the energy range 200 < E_gamma < 800 MeV. The experiment used a 4$\pi$ detection system, a circularly polarized tagged photon beam and a frozen spin target. The contributions to the Gerasimov-Drell-Hearn sum rule and to the forward spin polarizability $\gamma_0$ determined from the data are 226 \pm 5 (stat)\pm 12(sys) \mu b and -187 \pm 8 (stat)\pm 10(sys)10^{-6} fm^4, respectively, for 200 < E_\gamma < 800 MeV.Comment: 6 pages, 3 figures, 3 table

Expression and Characterization of Drosophila Signal Peptide Peptidase-Like (sppL), a Gene That Encodes an Intramembrane Protease

Intramembrane proteases of the Signal Peptide Peptidase (SPP) family play important roles in developmental, metabolic and signaling pathways. Although vertebrates have one SPP and four SPP-like (SPPL) genes, we found that insect genomes encode one Spp and one SppL. Characterization of the Drosophila sppL gene revealed that the predicted SppL protein is a highly conserved structural homolog of the vertebrate SPPL3 proteases, with a predicted nine-transmembrane topology, an active site containing aspartyl residues within a transmembrane region, and a carboxy-terminal PAL domain. SppL protein localized to both the Golgi and ER. Whereas spp is an essential gene that is required during early larval stages and whereas spp loss-of-function reduced the unfolded protein response (UPR), sppL loss of function had no apparent phenotype. This was unexpected given that genetic knockdown phenotypes in other organisms suggested significant roles for Spp-related proteases

The Loss of PGAM5 Suppresses the Mitochondrial Degeneration Caused by Inactivation of PINK1 in Drosophila

PTEN-induced kinase 1 (PINK1), which is required for mitochondrial homeostasis, is a gene product responsible for early-onset Parkinson's disease (PD). Another early onset PD gene product, Parkin, has been suggested to function downstream of the PINK1 signalling pathway based on genetic studies in Drosophila. PINK1 is a serine/threonine kinase with a predicted mitochondrial target sequence and a probable transmembrane domain at the N-terminus, while Parkin is a RING-finger protein with ubiquitin-ligase (E3) activity. However, how PINK1 and Parkin regulate mitochondrial activity is largely unknown. To explore the molecular mechanism underlying the interaction between PINK1 and Parkin, we biochemically purified PINK1-binding proteins from human cultured cells and screened the genes encoding these binding proteins using Drosophila PINK1 (dPINK1) models to isolate a molecule(s) involved in the PINK1 pathology. Here we report that a PINK1-binding mitochondrial protein, PGAM5, modulates the PINK1 pathway. Loss of Drosophila PGAM5 (dPGAM5) can suppress the muscle degeneration, motor defects, and shorter lifespan that result from dPINK1 inactivation and that can be attributed to mitochondrial degeneration. However, dPGAM5 inactivation fails to modulate the phenotypes of parkin mutant flies. Conversely, ectopic expression of dPGAM5 exacerbated the dPINK1 and Drosophila parkin (dParkin) phenotypes. These results suggest that PGAM5 negatively regulates the PINK1 pathway related to maintenance of the mitochondria and, furthermore, that PGAM5 acts between PINK1 and Parkin, or functions independently of Parkin downstream of PINK1

Helicity dependence of the γ→p→→nπ+π0 reaction in the second resonance region

The helicity dependence of the total cross section for the reaction has been measured for the first time at incident photon energies from 400 to 800 MeV. The measurement was performed with the large acceptance detector DAPHNE at the tagged photon beam facility of the MAMI accelerator in Mainz. This channel is found to be excited predominantly when the photon and proton have a parallel spin orientation, due to the intermediate production of the D13 resonance. peerReviewe