810 research outputs found

    From/To: G. Henry Towell (Chalk\u27s reply filed first)

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    Sea-quark flavor asymmetry in the nucleon from a relativistic analysis of the Drell-Yan scattering off nuclei

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    It is shown that accounting for the relativistic structure of the deuteron allows to explain the ratio of the Drell-Yan pair production cross-section at the low Bjorken xx off the deuteron and the proton. Thus, the sea quark distributions in the nucleon should be studied with accounting for the effects of the relativistic structure of the deuteron. The suggested approach reduces theoretical uncertainty in extracting the ratio uˉ/dˉ\bar u/\bar d from the data and it is important for the clarification of the nature of the sea quark asymmetry in the nucleon.Comment: 4 pages, 1 figures, Chiral Symmetry in Hadron and Nuclear Physics November 13-16, 2007, Osak

    Rare-earth distributions in some rocks and associated minerals of the batholith of southern California

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    Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Geology, 1963.Vita.Includes bibliographical references (leaves 170-175).by David Garrett Towell.Ph.D

    Order αs2\alpha_s^2 perturbative QCD corrections to the Gottfried sum rule

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    The order αs2\alpha_s^2 perturbative QCD correction to the Gottfried sum rule is obtained. The result is based on numerical calculation of the order αs2\alpha_s^2 contribution to the coefficient function and on the new estimate of the three-loop anomalous dimension term. The correction found is negative and rather small. Therefore it does not affect the necessity to introduce flavour-asymmetry between uˉ\bar{u} and dˉ\bar{d} antiquarks for the description of NMC result for the Gottfried sum rule.Comment: LaTeX, 7 pages, the discussions of the αs2\alpha_s^2 corrections to the anomalous dimension are modified; 1 reference added; to be published in Phys. Lett.

    Hunting for CDF Multi-Muon "Ghost" Events at Collider and Fixed-Target Experiments

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    In 2008 the CDF collaboration discovered a large excess of events containing two or more muons, at least one of which seemed to have been produced outside the beam pipe. We investigate whether similar "ghost" events could (and should) have been seen in already completed experiments. The CDF di-muon data can be reproduced by a simple model where a relatively light X particle undergoes four-body decay. This model predicts a large number of ghost events in Fermilab fixed-target experiments E772, E789 and E866, applying the cuts optimized for analyses of Drell-Yan events. A correct description of events with more than two muons requires a more complicated model, where two X particles are produced from a very broad resonance Y. This model can be tested in fixed-target experiments only if the cut on the angles, or rapidities, of the muons can be relaxed. Either way, the UA1 experiment at the CERN ppbar collider should have observed O(100) ghost events.Comment: 15 pages, 9 figure

    Staphylococcal Periscope proteins Aap, SasG, and Pls project noncanonical legume-like lectin adhesin domains from the bacterial surface

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    Staphylococcus aureus and Staphylococcus epidermidis are frequently associated with medical device infections that involve establishment of a bacterial biofilm on the device surface. Staphylococcal surface proteins Aap, SasG, and Pls are members of the Periscope Protein class and have been implicated in biofilm formation and host colonization; they comprise a repetitive region ("B region") and an N-terminal host colonization domain within the "A region," predicted to be a lectin domain. Repetitive E-G5 domains (as found in Aap, SasG, and Pls) form elongated "stalks" that would vary in length with repeat number, resulting in projection of the N-terminal A domain variable distances from the bacterial cell surface. Here, we present the structures of the lectin domains within A regions of SasG, Aap, and Pls and a structure of the Aap lectin domain attached to contiguous E-G5 repeats, suggesting the lectin domains will sit at the tip of the variable length rod. We demonstrate that these isolated domains (Aap, SasG) are sufficient to bind to human host desquamated nasal epithelial cells. Previously, proteolytic cleavage or a deletion within the A domain had been reported to induce biofilm formation; the structures suggest a potential link between these observations. Intriguingly, while the Aap, SasG, and Pls lectin domains bind a metal ion, they lack the nonproline cis peptide bond thought to be key for carbohydrate binding by the lectin fold. This suggestion of noncanonical ligand binding should be a key consideration when investigating the host cell interactions of these bacterial surface proteins
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