916 research outputs found

    Cuprous Oxide as a Catalyst. II. Adsorption by Cuprous Oxide

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    In a previous paper3, data were presented which demonstrated that cuprous oxide, prepared by the glucose reduction of a cupric nitrate solution at temperatures below 85°, was an active catalyst for the hydrogenation of furfural to furfuryl alcohol. It was also shown that the cuprous oxide was promoted by the addition of calcium oxide and vanadium tetroxidc. The most active mixture contained these oxides in the ratio Cu2O: V204: CaO: : 1.0: 0.71: 1.4. In order to elucidate the role played by the catalyst in the hydrogenation of furfural, the absorptive capacity of the catalyst for furfural and furfuryl alcohol was investigated. Previous work by Stanerson4 had shown that the catalyst would adsorb hydrogen in an irreversible manner at temperatures above 56° C. The authors found that the adsorption of hydrogen may be complicated by reduction of the cuprous oxide component of the catalyst to metallic copper

    Thermal Stability of RNA Phage Virus-Like Particles Displaying Foreign Peptides

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    <p>Abstract</p> <p>Background</p> <p>To be useful for genetic display of foreign peptides a viral coat protein must tolerate peptide insertions without major disruption of subunit folding and capsid assembly. The folding of the coat protein of RNA phage MS2 does not normally tolerate insertions in its AB-loop, but an engineered single-chain dimer readily accepts them as long as they are restricted to one of its two halves.</p> <p>Results</p> <p>Here we characterize the effects of peptide insertions on the thermal stabilities of MS2 virus-like particles (VLPs) displaying a variety of different peptides in one AB-loop of the coat protein single-chain dimer. These particles typically denature at temperatures around 5-10°C lower than unmodified VLPs. Even so, they are generally stable up to about 50°C. VLPs of the related RNA phage PP7 are cross-linked with intersubunit disulfide bonds and are therefore significantly more stable. An AB-loop insertion also reduces the stability of PP7 VLPs, but they only begin to denature above about 70°C.</p> <p>Conclusions</p> <p>VLPs assembled from MS2 single-chain dimer coat proteins with peptide insertions in one of their AB-loops are somewhat less stable than the wild-type particle, but still resist heating up to about 50°C. Because they possess disulfide cross-links, PP7-derived VLPs provide an alternate platform with even higher stability.</p

    Stability and assembly in vitro of bacteriophage PP7 virus-like particles

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    <p>Abstract</p> <p>Background</p> <p>The stability of a virus-like particle (VLP) is an important consideration for its use in nanobiotechnology. The icosahedral capsid of the RNA bacteriophage PP7 is cross-linked by disulfide bonds between coat protein dimers at its 5-fold and quasi-6-fold symmetry axes. This work determined the effects of these disulfides on the VLP's thermal stability.</p> <p>Results</p> <p>Measurements of the thermal denaturation behavior of PP7 VLPs in the presence and absence of a reducing agent show that disulfide cross-links substantially stabilize them against thermal denaturation. Although dimers in the capsid are linked to one another by disulfides, the two subunits of dimers themselves are held together only by non-covalent interactions. In an effort to confer even greater stability a new cross-link was introduced by genetically fusing two coat protein monomers, thus producing a "single-chain dimer" that assembles normally into a completely cross-linked VLP. However, subunit fusion failed to increase the thermal stability of the particles, even though it stabilized the isolated dimer. As a step toward gaining control of the internal composition of the capsid, conditions that promote the assembly of PP7 coat protein dimers into virus-like particles <it>in vitro </it>were established.</p> <p>Conclusion</p> <p>The presence of inter-dimer disulfide bonds greatly stabilizes the PP7 virus-like particle against thermal denaturation. Covalently cross-linking the subunits of the dimers themselves by genetically fusing them through a dipeptide linker sequence, offers no further stabilization of the VLP, although it does stabilize the dimer. PP7 capsids readily assemble <it>in vitro </it>in a reaction that requires RNA.</p

    Interference measurements of non-Abelian e/4 & Abelian e/2 quasiparticle braiding

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    The quantum Hall states at filling factors ν=5/2\nu=5/2 and 7/27/2 are expected to have Abelian charge e/2e/2 quasiparticles and non-Abelian charge e/4e/4 quasiparticles. For the first time we report experimental evidence for the non-Abelian nature of excitations at ν=7/2\nu=7/2 and examine the fermion parity, a topological quantum number of an even number of non-Abelian quasiparticles, by measuring resistance oscillations as a function of magnetic field in Fabry-P\'erot interferometers using new high purity heterostructures. The phase of observed e/4e/4 oscillations is reproducible and stable over long times (hours) near ν=5/2\nu=5/2 and 7/27/2, indicating stability of the fermion parity. When phase fluctuations are observed, they are predominantly π\pi phase flips, consistent with fermion parity change. We also examine lower-frequency oscillations attributable to Abelian interference processes in both states. Taken together, these results constitute new evidence for the non-Abelian nature of e/4e/4 quasiparticles; the observed life-time of their combined fermion parity further strengthens the case for their utility for topological quantum computation.Comment: A significantly revised version; 54 double-column pages containing 14 pages of main text + Supplementary Materials. The figures, which include a number of new figures, are now incorporated into the tex

    Fast Collision Course Vectoring

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    Control Systems Laboratory changed its name to Coordinated Science LaboratoryContract DA-36-039-SC-5669

    Understanding the Use of Prostate Biopsy Among Men with Limited Life Expectancy in a Statewide Quality Improvement Collaborative

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    BACKGROUND: The potential harms of a prostate cancer (PCa) diagnosis may outweigh its benefits in elderly men. OBJECTIVE: To assess the use of prostate biopsy in men with limited life expectancy (LE) within the practices comprising the Michigan Urological Surgery Improvement Collaborative (MUSIC). DESIGN, SETTING, AND PARTICIPANTS: MUSIC is a consortium of 42 practices and nearly 85% of the urologists in Michigan. From July 2013 to October 2014, clinical data were collected prospectively for all men undergoing prostate biopsy. OUTCOME MEASUREMENTS AND STATISTICAL ANALYSIS: We calculated comorbidity-adjusted LE in men aged ≥66 yr and identified men with(limited LE) undergoing a first biopsy. Our LE calculator was not designed for men agedyr; thus these men were excluded. Multivariable models estimated the proportion of all biopsies performed for men with limited LE in each MUSIC practice, adjusting for differences in patient characteristics. We also evaluated what treatments, if any, these patients received. RESULTS AND LIMITATIONS: Among 3035 men aged ≥66 yr undergoing initial prostate biopsy, 60% had none of the measured comorbidities. Overall, 547 men (18%) had limited LE. Compared with men with a longer LE, these men had significantly higher prostate-specific antigen levels and abnormal digital rectal examination findings. The adjusted proportion of biopsies performed for men with limited LE ranged from 3.8% to 39% across MUSIC practices (p \u3c 0.001). PCa was diagnosed in 69% of men with limited LE; among this group, 74% received any active treatment. Of these men, 46% had high-grade cancer (Gleason score 8-10). CONCLUSIONS: Among a large and diverse group of urology practices, nearly 20% of prostate biopsies are performed in men with limited LE. These data provide useful context for quality improvement efforts aimed at optimizing patient selection for prostate biopsy. PATIENT SUMMARY: In this report, nearly 2 of every 10 men undergoing prostate biopsy had a life expectancy (LE)biopsy

    A malaria vaccine candidate based on an epitope of the Plasmodium falciparum RH5 protein

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    BACKGROUND: The Plasmodium falciparum protein RH5 is an adhesin molecule essential for parasite invasion of erythrocytes. Recent studies show that anti-PfRH5 sera have potent invasion-inhibiting activities, supporting the idea that the PfRH5 antigen could form the basis of a vaccine. Therefore, epitopes recognized by neutralizing anti-PfRH5 antibodies could themselves be effective vaccine immunogens if presented in a sufficiently immunogenic fashion. However, the exact regions within PfRH5 that are targets of this invasion-inhibitory activity have yet to be identified. METHODS: A battery of anti-RH5 monoclonal antibodies (mAbs) were produced and screened for their potency by inhibition of invasion assays in vitro. Using an anti-RH5 mAb that completely inhibited invasion as the selecting mAb, affinity-selection using random sequence peptide libraries displayed on virus-like particles of bacteriophage MS2 (MS2 VLPs) was performed. VLPs were sequenced to identify the specific peptide epitopes they encoded and used to raise specific antisera that was in turn tested for inhibition of invasion. RESULTS: Three anti-RH5 monoclonals (0.1 mg/mL) were able to inhibit invasion in vitro by >95%. Affinity-selection with one of these mAbs yielded a VLP which yielded a peptide whose sequence is identical to a portion of PfRH5 itself. The VLP displaying the peptide binds strongly to the antibody, and in immunized animals elicits an anti-PfRH5 antibody response. The resulting antisera against the specific VLP inhibit parasite invasion of erythrocytes more than 90% in vitro. CONCLUSIONS: Here, data is presented from an anti-PfRH5 mAb that completely inhibits erythrocyte invasion by parasites in vitro, one of the few anti-malarial monoclonal antibodies reported to date that completely inhibits invasion with such potency, adding to other studies that highlight the potential of PfRH5 as a vaccine antigen. The specific neutralization sensitive epitope within RH5 has been identified, and antibodies against this epitope also elicit high anti-invasion activity, suggesting this epitope could form the basis of an effective vaccine against malaria
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