1,620 research outputs found

    Analog of the Clauser-Horne-Shimony-Holt inequality for steering

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    The Clauser-Horne-Shimony-Holt (CHSH) inequality (and its permutations), are necessary and sufficient criteria for Bell nonlocality in the simplest Bell-nonlocality scenario: 2 parties, 2 measurements per party and 2 outcomes per measurement. Here we derive an inequality for EPR-steering that is an analogue of the CHSH, in that it is necessary and sufficient in this same scenario. However, since in the case of steering the device at Bob's site must be specified (as opposed to the Bell case in which it is a black box), the scenario we consider is that where Alice performs two (black-box) dichotomic measurements, and Bob performs two mutually unbiased qubit measurements. We show that this inequality is strictly weaker than the CHSH, as expected, and use it to decide whether a recent experiment [Phys. Rev. Lett. 110, 130401 (2013).] involving a single-photon split between two parties has demonstrated EPR-steering.Comment: Expanded v2, new results, new figure. 9 pages, 2 figure

    Identification of protein complexes with quantitative proteomics in S. cerevisiae

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    Lipids are the building blocks of cellular membranes that function as barriers and in compartmentalization of cellular processes, and recently, as important intracellular signalling molecules. However, unlike proteins, lipids are small hydrophobic molecules that traffic primarily by poorly described nonvesicular routes, which are hypothesized to occur at membrane contact sites (MCSs). MCSs are regions where the endoplasmic reticulum (ER) makes direct physical contact with a partnering organelle, e.g., plasma membrane (PM). The ER portion of ER-PM MCSs is enriched in lipid-synthesizing enzymes, suggesting that lipid synthesis is directed to these sites and implying that MCSs are important for lipid traffic. Yeast is an ideal model to study ER-PM MCSs because of their abundance, with over 1000 contacts per cell, and their conserved nature in all eukaryotes. Uncovering the proteins that constitute MCSs is critical to understanding how lipids traffic is accomplished in cells, and how they act as signaling molecules. We have found that an ER called Scs2p localize to ER-PM MCSs and is important for their formation. We are focused on uncovering the molecular partners of Scs2p. Identification of protein complexes traditionally relies on first resolving purified protein samples by gel electrophoresis, followed by in-gel digestion of protein bands and analysis of peptides by mass spectrometry. This often limits the study to a small subset of proteins. Also, protein complexes are exposed to denaturing or non-physiological conditions during the procedure. To circumvent these problems, we have implemented a large-scale quantitative proteomics technique to extract unbiased and quantified data. We use stable isotope labeling with amino acids in cell culture (SILAC) to incorporate staple isotope nuclei in proteins in an untagged control strain. Equal volumes of tagged culture and untagged, SILAC-labeled culture are mixed together and lysed by grinding in liquid nitrogen. We then carry out an affinity purification procedure to pull down protein complexes. Finally, we precipitate the protein sample, which is ready for analysis by high-performance liquid chromatography/ tandem mass spectrometry. Most importantly, proteins in the control strain are labeled by the heavy isotope and will produce a mass/ charge shift that can be quantified against the unlabeled proteins in the bait strain. Therefore, contaminants, or unspecific binding can be easily eliminated. By using this approach, we have identified several novel proteins that localize to ER-PM MCSs. Here we present a detailed description of our approach

    Vortex pairing in two-dimensional Bose gases

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    Recent experiments on ultracold Bose gases in two dimensions have provided evidence for the existence of the Berezinskii-Kosterlitz-Thouless (BKT) phase via analysis of the interference between two independent systems. In this work we study the two-dimensional quantum degenerate Bose gas at finite temperature using the projected Gross-Pitaevskii equation classical field method. While this describes the highly occupied modes of the gas below a momentum cutoff, we have developed a method to incorporate the higher momentum states in our model. We concentrate on finite-sized homogeneous systems in order to simplify the analysis of the vortex pairing. We determine the dependence of the condensate fraction on temperature and compare this to the calculated superfluid fraction. By measuring the first order correlation function we determine the boundary of the Bose-Einstein condensate and BKT phases, and find it is consistent with the superfluid fraction decreasing to zero. We reveal the characteristic unbinding of vortex pairs above the BKT transition via a coarse-graining procedure. Finally, we model the procedure used in experiments to infer system correlations [Hadzibabic et al., Nature 441, 1118 (2006)], and quantify its level of agreement with directly calculated in situ correlation functions.Comment: published versio

    Assembly of the Complex between Archaeal RNase P Proteins RPP30 and Pop5

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    RNase P is a highly conserved ribonucleoprotein enzyme that represents a model complex for understanding macromolecular RNA-protein interactions. Archaeal RNase P consists of one RNA and up to five proteins (Pop5, RPP30, RPP21, RPP29, and RPP38/L7Ae). Four of these proteins function in pairs (Pop5-RPP30 and RPP21–RPP29). We have used nuclear magnetic resonance (NMR) spectroscopy and isothermal titration calorimetry (ITC) to characterize the interaction between Pop5 and RPP30 from the hyperthermophilic archaeon Pyrococcus furiosus (Pfu). NMR backbone resonance assignments of free RPP30 (25 kDa) indicate that the protein is well structured in solution, with a secondary structure matching that observed in a closely related crystal structure. Chemical shift perturbations upon the addition of Pop5 (14 kDa) reveal its binding surface on RPP30. ITC experiments confirm a net 1 : 1 stoichiometry for this tight protein-protein interaction and exhibit complex isotherms, indicative of higher-order binding. Indeed, light scattering and size exclusion chromatography data reveal the complex to exist as a 78 kDa heterotetramer with two copies each of Pop5 and RPP30. These results will inform future efforts to elucidate the functional role of the Pop5-RPP30 complex in RNase P assembly and catalysis
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