1,448 research outputs found

    Lattice study on ηc2\eta_{c2} and X(3872)

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    Properties of 2+2^{-+} charmonium ηc2\eta_{c2} are investigated in quenched lattice QCD. The mass of ηc2\eta_{c2} is determined to be 3.80(3) GeV, which is close to the mass of DD-wave charmonium ψ(3770)\psi(3770) and in agreement with quark model predictions. The transition width of ηc2γJ/ψ\eta_{c2}\to \gamma J/\psi is also obtained with a value Γ=3.8(9)\Gamma=3.8(9) keV. Since the possible 2+2^{-+} assignment to X(3872) has not been ruled out by experiments, our results help to clarify the nature of X(3872).Comment: 15 pages, 8 figures. typos, grammatical errors and some references corrected, redundant discussions deleted, conclusion does not change. published versio

    2-Chloro-1-(4,5,6,7-tetrahydro­thieno[3,2-c]pyridin-5-yl)ethanone

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    In the title compound, C9H10ClNOS, the dihedral angle between the planar thio­phene ring and 2-chloro­ethane moiety (r.m.s deviations of 0.003 and 0.015 Å, respectively) is 45.79 (6)°. The tetra­hydro­pyridine ring adopts a half-chair conformation. The crystal packing reveals inter­molecular C—H⋯O inter­actions

    Neutron star phase transition as the origin for the fast radio bursts and soft gamma-ray repeaters of SGR J1935+2154

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    Magnetars are believed as neutron stars (NSs) with strong magnetic fields. X-ray flares and fast radio bursts (FRBs) have been observed from the magnetar (soft gamma-ray repeater, SGR J1935+2154). We propose that the phase transition of the NS can power the FRBs and SGRs.Based on the equation of state provided by the MIT bag model and the mean field approximation, we solve the Tolman-Oppenheimer-Volkoff equations to get the NS structure. With spin-down of the NS, the hadronic shell gradually transfers to the quark shell.The gravitational potential energy released by one time of the phase transition can be achieved. The released energy, time interval between two successive phase transitions, and glitch are all consistent with the observations of the FRBs and the X-ray flares from SGR J1935+2154. We conclude that the phase transition of an NS is a plausible mechanism to power the SGRs as well as the repeating FRBs.Comment: 11 pages, 3 figure

    The exchanged EF-hands in calmodulin and troponin C chimeras impair the Ca2+-induced hydrophobicity and alter the interaction with Orai1: a spectroscopic, thermodynamic and kinetic study

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    Background Calmodulin (CaM) plays an important role in Ca2+-dependent signal transduction. Ca2+ binding to CaM triggers a conformational change, forming a hydrophobic patch that is important for target protein recognition. CaM regulates a Ca2+-dependent inactivation process in store-operated Ca2+entry, by interacting Orai1. To understand the relationship between Ca2+-induced hydrophobicity and CaM/Orai interaction, chimera proteins constructed by exchanging EF-hands of CaM with those of Troponin C (TnC) are used as an informative probe to better understand the functionality of each EF-hand. Results ANS was used to assess the context of the induced hydrophobic surface on CaM and chimeras upon Ca2+ binding. The exchanged EF-hands from TnC to CaM resulted in reduced hydrophobicity compared with wild-type CaM. ANS lifetime measurements indicated that there are two types of ANS molecules with rather distinct fluorescence lifetimes, each specifically corresponding to one lobe of CaM or chimeras. Thermodynamic studies indicated the interaction between CaM and a 24-residue peptide corresponding to the CaM-binding domain of Orail1 (Orai-CMBD) is a 1:2 CaM/Orai-CMBD binding, in which each peptide binding yields a similar enthalpy change (ΔH = −5.02 ± 0.13 kcal/mol) and binding affinity (Ka = 8.92 ± 1.03 × 105 M−1). With the exchanged EF1 and EF2, the resulting chimeras noted as CaM(1TnC) and CaM(2TnC), displayed a two sequential binding mode with a one-order weaker binding affinity and lower ΔH than that of CaM, while CaM(3TnC) and CaM(4TnC) had similar binding thermodynamics as CaM. The dissociation rate constant for CaM/Orai-CMBD was determined to be 1.41 ± 0.08 s−1 by rapid kinetics. Stern-Volmer plots of Orai-CMBD Trp76 indicated that the residue is located in a very hydrophobic environment but becomes more solvent accessible when EF1 and EF2 were exchanged. Conclusions Using ANS dye to assess induced hydrophobicity showed that exchanging EFs for all Ca2+-bound chimeras impaired ANS fluorescence and/or binding affinity, consistent with general concepts about the inadequacy of hydrophobic exposure for chimeras. However, such ANS responses exhibited no correlation with the ability to interact with Orai-CMBD. Here, the model of 1:2 binding stoichiometry of CaM/Orai-CMBD established in solution supports the already published crystal structure

    Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar

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    <p>Abstract</p> <p>Background</p> <p>Although there has been considerable progress made towards understanding the molecular mechanisms of bud dormancy, the roles of protein phosphorylation in the process of dormancy regulation in woody plants remain unclear.</p> <p>Results</p> <p>We used mass spectrometry combined with TiO<sub>2 </sub>phosphopeptide-enrichment strategies to investigate the phosphoproteome of dormant terminal buds (DTBs) in poplar (<it>Populus simonii × P. nigra</it>). There were 161 unique phosphorylated sites in 161 phosphopeptides from 151 proteins; 141 proteins have orthologs in <it>Arabidopsis</it>, and 10 proteins are unique to poplar. Only 34 sites in proteins in poplar did not match well with the equivalent phosphorylation sites of their orthologs in <it>Arabidopsis</it>, indicating that regulatory mechanisms are well conserved between poplar and <it>Arabidopsis</it>. Further functional classifications showed that most of these phosphoproteins were involved in binding and catalytic activity. Extraction of the phosphorylation motif using Motif-X indicated that proline-directed kinases are a major kinase group involved in protein phosphorylation in dormant poplar tissues.</p> <p>Conclusions</p> <p>This study provides evidence about the significance of protein phosphorylation during dormancy, and will be useful for similar studies on other woody plants.</p
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