1,174 research outputs found
Magnetic Properties of FePt Nanoparticles Prepared by a Micellar Method
FePt nanoparticles with average size of 9 nm were synthesized using a diblock polymer micellar method combined with plasma treatment. To prevent from oxidation under ambient conditions, immediately after plasma treatment, the FePt nanoparticle arrays were in situ transferred into the film-growth chamber where they were covered by an SiO2 overlayer. A nearly complete transformation of L10 FePt was achieved for samples annealed at temperatures above 700 °C. The well control on the FePt stoichiometry and avoidance from surface oxidation largely enhanced the coercivity, and a value as high as 10 kOe was obtained in this study. An evaluation of magnetic interactions was made using the so-called isothermal remanence (IRM) and dc-demagnetization (DCD) remanence curves and Kelly–Henkel plots (ΔM measurement). The ΔM measurement reveals that the resultant FePt nanoparticles exhibit a rather weak interparticle dipolar coupling, and the absence of interparticle exchange interaction suggests no significant particle agglomeration occurred during the post-annealing. Additionally, a slight parallel magnetic anisotropy was also observed. The results indicate the micellar method has a high potential in preparing FePt nanoparticle arrays used for ultrahigh density recording media
Study on Composition Distribution and Ferromagnetism of Monodisperse FePt Nanoparticles
Monodisperse FePt nanoparticles with size of 4.5 and 6.0 nm were prepared by simultaneous reduction of platinum acetylacetonate and thermal decomposition of iron pentacarbonyl in benzylether. The crystallography structure, size, and composition of the FePt nanoparticles were examined by X-ray diffraction and transmission electron microscopy. Energy dispersive X-ray spectrometry measurements of individual particles indicate a broad compositional distribution in both the 4.5 and 6 nm FePt nanoparticles. The effects of compositional distribution on the phase-transition and magnetic properties of the FePt nanoparticles were investigated
JUNO Conceptual Design Report
The Jiangmen Underground Neutrino Observatory (JUNO) is proposed to determine
the neutrino mass hierarchy using an underground liquid scintillator detector.
It is located 53 km away from both Yangjiang and Taishan Nuclear Power Plants
in Guangdong, China. The experimental hall, spanning more than 50 meters, is
under a granite mountain of over 700 m overburden. Within six years of running,
the detection of reactor antineutrinos can resolve the neutrino mass hierarchy
at a confidence level of 3-4, and determine neutrino oscillation
parameters , , and to
an accuracy of better than 1%. The JUNO detector can be also used to study
terrestrial and extra-terrestrial neutrinos and new physics beyond the Standard
Model. The central detector contains 20,000 tons liquid scintillator with an
acrylic sphere of 35 m in diameter. 17,000 508-mm diameter PMTs with high
quantum efficiency provide 75% optical coverage. The current choice of
the liquid scintillator is: linear alkyl benzene (LAB) as the solvent, plus PPO
as the scintillation fluor and a wavelength-shifter (Bis-MSB). The number of
detected photoelectrons per MeV is larger than 1,100 and the energy resolution
is expected to be 3% at 1 MeV. The calibration system is designed to deploy
multiple sources to cover the entire energy range of reactor antineutrinos, and
to achieve a full-volume position coverage inside the detector. The veto system
is used for muon detection, muon induced background study and reduction. It
consists of a Water Cherenkov detector and a Top Tracker system. The readout
system, the detector control system and the offline system insure efficient and
stable data acquisition and processing.Comment: 328 pages, 211 figure
Measurements of branching fraction ratios and CP-asymmetries in suppressed B^- -> D(-> K^+ pi^-)K^- and B^- -> D(-> K^+ pi^-)pi^- decays
We report the first reconstruction in hadron collisions of the suppressed
decays B^- -> D(-> K^+ pi^-)K^- and B^- -> D(-> K^+ pi^-)pi^-, sensitive to the
CKM phase gamma, using data from 7 fb^-1 of integrated luminosity collected by
the CDF II detector at the Tevatron collider. We reconstruct a signal for the
B^- -> D(-> K^+ pi^-)K^- suppressed mode with a significance of 3.2 standard
deviations, and measure the ratios of the suppressed to favored branching
fractions R(K) = [22.0 \pm 8.6(stat)\pm 2.6(syst)]\times 10^-3, R^+(K) =
[42.6\pm 13.7(stat)\pm 2.8(syst)]\times 10^-3, R^-(K)= [3.8\pm 10.3(stat)\pm
2.7(syst]\times 10^-3, as well as the direct CP-violating asymmetry A(K) =
-0.82\pm 0.44(stat)\pm 0.09(syst) of this mode. Corresponding quantities for
B^- -> D(-> K^+ pi^-)pi^- decay are also reported.Comment: 8 pages, 1 figure, accepted by Phys.Rev.D Rapid Communications for
Publicatio
Observation of an Excited Bc+ State
Using pp collision data corresponding to an integrated luminosity of 8.5 fb-1 recorded by the LHCb experiment at center-of-mass energies of s=7, 8, and 13 TeV, the observation of an excited Bc+ state in the Bc+π+π- invariant-mass spectrum is reported. The observed peak has a mass of 6841.2±0.6(stat)±0.1(syst)±0.8(Bc+) MeV/c2, where the last uncertainty is due to the limited knowledge of the Bc+ mass. It is consistent with expectations of the Bc∗(2S31)+ state reconstructed without the low-energy photon from the Bc∗(1S31)+→Bc+γ decay following Bc∗(2S31)+→Bc∗(1S31)+π+π-. A second state is seen with a global (local) statistical significance of 2.2σ (3.2σ) and a mass of 6872.1±1.3(stat)±0.1(syst)±0.8(Bc+) MeV/c2, and is consistent with the Bc(2S10)+ state. These mass measurements are the most precise to date
The Drosophila melanogaster PeptideAtlas facilitates the use of peptide data for improved fly proteomics and genome annotation
<p>Abstract</p> <p>Background</p> <p>Crucial foundations of any quantitative systems biology experiment are correct genome and proteome annotations. Protein databases compiled from high quality empirical protein identifications that are in turn based on correct gene models increase the correctness, sensitivity, and quantitative accuracy of systems biology genome-scale experiments.</p> <p>Results</p> <p>In this manuscript, we present the <it>Drosophila melanogaster </it>PeptideAtlas, a fly proteomics and genomics resource of unsurpassed depth. Based on peptide mass spectrometry data collected in our laboratory the portal <url>http://www.drosophila-peptideatlas.org</url> allows querying fly protein data observed with respect to gene model confirmation and splice site verification as well as for the identification of proteotypic peptides suited for targeted proteomics studies. Additionally, the database provides consensus mass spectra for observed peptides along with qualitative and quantitative information about the number of observations of a particular peptide and the sample(s) in which it was observed.</p> <p>Conclusion</p> <p>PeptideAtlas is an open access database for the <it>Drosophila </it>community that has several features and applications that support (1) reduction of the complexity inherently associated with performing targeted proteomic studies, (2) designing and accelerating shotgun proteomics experiments, (3) confirming or questioning gene models, and (4) adjusting gene models such that they are in line with observed <it>Drosophila </it>peptides. While the database consists of proteomic data it is not required that the user is a proteomics expert.</p
Sorting Signals, N-Terminal Modifications and Abundance of the Chloroplast Proteome
Characterization of the chloroplast proteome is needed to understand the essential contribution of the chloroplast to plant growth and development. Here we present a large scale analysis by nanoLC-Q-TOF and nanoLC-LTQ-Orbitrap mass spectrometry (MS) of ten independent chloroplast preparations from Arabidopsis thaliana which unambiguously identified 1325 proteins. Novel proteins include various kinases and putative nucleotide binding proteins. Based on repeated and independent MS based protein identifications requiring multiple matched peptide sequences, as well as literature, 916 nuclear-encoded proteins were assigned with high confidence to the plastid, of which 86% had a predicted chloroplast transit peptide (cTP). The protein abundance of soluble stromal proteins was calculated from normalized spectral counts from LTQ-Obitrap analysis and was found to cover four orders of magnitude. Comparison to gel-based quantification demonstrates that ‘spectral counting’ can provide large scale protein quantification for Arabidopsis. This quantitative information was used to determine possible biases for protein targeting prediction by TargetP and also to understand the significance of protein contaminants. The abundance data for 550 stromal proteins was used to understand abundance of metabolic pathways and chloroplast processes. We highlight the abundance of 48 stromal proteins involved in post-translational proteome homeostasis (including aminopeptidases, proteases, deformylases, chaperones, protein sorting components) and discuss the biological implications. N-terminal modifications were identified for a subset of nuclear- and chloroplast-encoded proteins and a novel N-terminal acetylation motif was discovered. Analysis of cTPs and their cleavage sites of Arabidopsis chloroplast proteins, as well as their predicted rice homologues, identified new species-dependent features, which will facilitate improved subcellular localization prediction. No evidence was found for suggested targeting via the secretory system. This study provides the most comprehensive chloroplast proteome analysis to date and an expanded Plant Proteome Database (PPDB) in which all MS data are projected on identified gene models
Dynamics of notch pathway expression during mouse testis post-natal development and along the spermatogenic cycle
Articles in International JournalsThe transcription and expression patterns of Notch pathway components (Notch 1–3, Delta1 and 4, Jagged1) and effectors
(Hes1, Hes2, Hes5 and Nrarp) were evaluated (through RT-PCR and IHC) in the mouse testis at key moments of post-natal
development, and along the adult spermatogenic cycle. Notch pathway components and effectors are transcribed in the
testis and expressed in germ, Sertoli and Leydig cells, and each Notch component shows a specific cell-type and timewindow
expression pattern. This expression at key testis developmental events prompt for a role of Notch signaling in prepubertal
spermatogonia quiescence, onset of spermatogenesis, and regulation of the spermatogenic cycle
A Mighty Small Heart: The Cardiac Proteome of Adult Drosophila melanogaster
Drosophila melanogaster is emerging as a powerful model system
for the study of cardiac disease. Establishing peptide and protein maps of the
Drosophila heart is central to implementation of protein
network studies that will allow us to assess the hallmarks of
Drosophila heart pathogenesis and gauge the degree of
conservation with human disease mechanisms on a systems level. Using a
gel-LC-MS/MS approach, we identified 1228 protein clusters from 145 dissected
adult fly hearts. Contractile, cytostructural and mitochondrial proteins were
most abundant consistent with electron micrographs of the
Drosophila cardiac tube. Functional/Ontological enrichment
analysis further showed that proteins involved in glycolysis,
Ca2+-binding, redox, and G-protein signaling, among other
processes, are also over-represented. Comparison with a mouse heart proteome
revealed conservation at the level of molecular function, biological processes
and cellular components. The subsisting peptidome encompassed 5169 distinct
heart-associated peptides, of which 1293 (25%) had not been identified in
a recent Drosophila peptide compendium. PeptideClassifier
analysis was further used to map peptides to specific gene-models. 1872 peptides
provide valuable information about protein isoform groups whereas a further 3112
uniquely identify specific protein isoforms and may be used as a
heart-associated peptide resource for quantitative proteomic approaches based on
multiple-reaction monitoring. In summary, identification of
excitation-contraction protein landmarks, orthologues of proteins associated
with cardiovascular defects, and conservation of protein ontologies, provides
testimony to the heart-like character of the Drosophila cardiac
tube and to the utility of proteomics as a complement to the power of genetics
in this growing model of human heart disease
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