972 resultados para Boston (Mass.). Church of Humanity.


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The records provide material relating to the accreditation, fundraising, management, planning, policies, programs, and public relations of a hospital that continues to serve the Greater Boston area. The records includes correspondence of various Presidents, Board Members, and Executive Directors; Board and committee minutes; scrapbooks, photographs, videotape, and film created by the Public Relations department; records of various Auxiliary groups; correspondence, reports, surveys, and other documents relating to the Pediatric Rehabilitation Program; and artifacts such as plaques, portraits, and silverware.

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In 1916, the Jewish community of Boston established Beth Israel Hospital on Townsend Street in Roxbury to provide health care to immigrants in the area. Although accessible to everyone, the hospital provided Yiddish-speaking services for Eastern European Jewish immigrants and served kosher food, as well as conducted Jewish religious services. In 1928 the hospital entered into a teaching agreement with Harvard Medical School, Tufts University, and Simmons College. Shortly thereafter, the hospital moved to its current location in the Longwood area of Boston and expanded to a 220-bed operation. During 1935-1936, at the height of the Depression, Beth Israel spent 1.5 million dollars in free patient care and was only one of two local hospitals to offer health care to people on welfare. In 1996, Beth Israel Hospital merged with Deaconess Medical Center and became Beth Israel Deaconess Medical Center. This collection contains reports, pamphlets and hospital publications.

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Temple Israel was founded as Congregation Adath Israel in 1854 when a group of German Jews broke from Congregation Ohabei Shalom. The congregation was also known as the Pleasant Street Synagogue. In 1859, the congregation purchased cemetery land in Wakefield, Massachusetts. The synagogue was, and remains, a Reform congregation, and has been home to well known Rabbis, including Joshua Loth Liebman and Roland B. Gittelsohn. This collection contains flyers, newsletters, pamphlets, sermons and a yearbook.

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Congregation Mishkan Tefila was founded in 1858 as Mishkan Israel, and is considered to be the oldest conservative synagogue in New England. Its founding members were East Prussian Jews who separated from Ohabei Shalom, which was predominately Polish at the time. In 1894, Mishkan Israel and another conservative synagogue, Shaarei Tefila, merged to form Congregation Mishkan Tefila. The synagogue moved its religious school to Walnut Street in Newton in 1955, and began planning for a new building in Chestnut Hill on Hammond Pond Parkway. The groundbreaking ceremony was on November 13, 1955. In 1958, services were held for the first time in the new synagogue building. This collection contains plays, annual reports, programs for events and dinners, and newsletters.

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We present a measurement of the top quark mass and of the top-antitop pair production cross section using p-pbar data collected with the CDFII detector at the Tevatron Collider at the Fermi National Accelerator Laboratory and corresponding to an integrated luminosity of 2.9 fb-1. We select events with six or more jets satisfying a number of kinematical requirements imposed by means of a neural network algorithm. At least one of these jets must originate from a b quark, as identified by the reconstruction of a secondary vertex inside the jet. The mass measurement is based on a likelihood fit incorporating reconstructed mass distributions representative of signal and background, where the absolute jet energy scale (JES) is measured simultaneously with the top quark mass. The measurement yields a value of 174.8 +- 2.4(stat+JES) ^{+1.2}_{-1.0}(syst) GeV/c^2, where the uncertainty from the absolute jet energy scale is evaluated together with the statistical uncertainty. The procedure measures also the amount of signal from which we derive a cross section, sigma_{ttbar} = 7.2 +- 0.5(stat) +- 1.0 (syst) +- 0.4 (lum) pb, for the measured values of top quark mass and JES.

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The binding of 1-anilino-8-naphthalene-sulfonic acid to globular proteins at acidic pH has been investigated by electrospray ionization mass spectrometry (ESIMS). Mass spectra of apomyoglobin recorded in the pH range 2−7 establish that maximal ANS binding is observed at pH 4.0. As many as seven distinct species may be observed in the gas phase which correspond to protein molecules containing one to six molecules of bound ANS. At neutral pH only a single molecule of ANS is bound. In the case of cytochrome c, maximal binding is observed at pH 4.0, with five molecules being bound. Binding is suppressed at neutral pH. In both cases ESIMS demonstrates maximal ANS binding at pH values where the proteins have been reported to exist in molten globule states. ANS binding is not observed for lysozyme, which has a tightly folded structure over the entire pH range. Reduction of disulfide bonds in lysozyme leads to the detection of ANS-bound species at neutral pH. Binding is suppressed at low pH due to complete unfolding of the reduced protein. The results suggest that ESIMS may provide a convenient method of probing the stoichiometry and distribution of dye complexes with molten protein globules

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Human sport doping control analysis is a complex and challenging task for anti-doping laboratories. The List of Prohibited Substances and Methods, updated annually by World Anti-Doping Agency (WADA), consists of hundreds of chemically and pharmacologically different low and high molecular weight compounds. This poses a considerable challenge for laboratories to analyze for them all in a limited amount of time from a limited sample aliquot. The continuous expansion of the Prohibited List obliges laboratories to keep their analytical methods updated and to research new available methodologies. In this thesis, an accurate mass-based analysis employing liquid chromatography - time-of-flight mass spectrometry (LC-TOFMS) was developed and validated to improve the power of doping control analysis. New analytical methods were developed utilizing the high mass accuracy and high information content obtained by TOFMS to generate comprehensive and generic screening procedures. The suitability of LC-TOFMS for comprehensive screening was demonstrated for the first time in the field with mass accuracies better than 1 mDa. Further attention was given to generic sample preparation, an essential part of screening analysis, to rationalize the whole work flow and minimize the need for several separate sample preparation methods. Utilizing both positive and negative ionization allowed the detection of almost 200 prohibited substances. Automatic data processing produced a Microsoft Excel based report highlighting the entries fulfilling the criteria of the reverse data base search (retention time (RT), mass accuracy, isotope match). The quantitative performance of LC-TOFMS was demonstrated with morphine, codeine and their intact glucuronide conjugates. After a straightforward sample preparation the compounds were analyzed directly without the need for hydrolysis, solvent transfer, evaporation or reconstitution. The hydrophilic interaction technique (HILIC) provided good chromatographic separation, which was critical for the morphine glucuronide isomers. A wide linear range (50-5000 ng/ml) with good precision (RSD<10%) and accuracy (±10%) was obtained, showing comparable or better performance to other methods used. In-source collision-induced dissociation (ISCID) allowed confirmation analysis with three diagnostic ions with a median mass accuracy of 1.08 mDa and repeatable ion ratios fulfilling WADA s identification criteria. The suitability of LC-TOFMS for screening of high molecular weight doping agents was demonstrated with plasma volume expanders (PVE), namely dextran and hydroxyethylstarch (HES). Specificity of the assay was improved, since interfering matrix compounds were removed by size exclusion chromatography (SEC). ISCID produced three characteristic ions with an excellent mean mass accuracy of 0.82 mDa at physiological concentration levels. In summary, by combining TOFMS with a proper sample preparation and chromatographic separation, the technique can be utilized extensively in doping control laboratories for comprehensive screening of chemically different low and high molecular weight compounds, for quantification of threshold substances and even for confirmation. LC-TOFMS rationalized the work flow in doping control laboratories by simplifying the screening scheme, expediting reporting and minimizing the analysis costs. Therefore LC-TOFMS can be exploited widely in doping control, and the need for several separate analysis techniques is reduced.

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Stellar mass black holes (SMBHs), forming by the core collapse of very massive, rapidly rotating stars, are expected to exhibit a high density accretion disk around them developed from the spinning mantle of the collapsing star. A wide class of such disks, due to their high density and temperature, are effective emitters of neutrinos and hence called neutrino cooled disks. Tracking the physics relating the observed (neutrino) luminosity to the mass, spin of black holes (BHs) and the accretion rate ((M) over dot) of such disks, here we establish a correlation between the spin and mass of SMBHs at their formation stage. Our work shows that spinning BHs are more massive than nonspinning BHs for a given (M) over dot. However, slowly spinning BHs can turn out to be more massive than spinning BHs if (M) over dot at their formation stage was higher compared to faster spinning BHs.

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The 2011 outburst of the black hole candidate IGR J17091-3624 followed the canonical track of state transitions along with the evolution of quasi-periodic oscillation (QPO) frequencies before it began exhibiting various variability classes similar to GRS 1915+105. We use this canonical evolution of spectral and temporal properties to determine the mass of IGR J17091-3624, using three different methods: photon index (Gamma)-QPO frequency (nu) correlation, QPO frequency (nu)-time (day) evolution, and broadband spectral modeling based on two-component advective flow (TCAF). We provide a combined mass estimate for the source using a naive Bayes based joint likelihood approach. This gives a probable mass range of 11.8 M-circle dot-13.7 M-circle dot. Considering each individual estimate and taking the lowermost and uppermost bounds among all three methods, we get a mass range of 8.7 M-circle dot-15.6 M-circle dot with 90% confidence. We discuss the possible implications of our findings in the context of two-component accretion flow.

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Contributed to: 4th International Conference, EuroMed 2012, Limassol, Cyprus, October 29 – November 3, 2012.

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We grow ultra-high mass density carbon nanotube forests at 450°C on Ti-coated Cu supports using Co-Mo co-catalyst. X-ray photoelectron spectroscopy shows Mo strongly interacts with Ti and Co, suppressing both aggregation and lifting off of Co particles and, thus, promoting the root growth mechanism. The forests average a height of 0.38 μm and a mass density of 1.6 g cm -3. This mass density is the highest reported so far, even at higher temperatures or on insulators. The forests and Cu supports show ohmic conductivity (lowest resistance ∼22 kΩ), suggesting Co-Mo is useful for applications requiring forest growth on conductors. © 2013 AIP Publishing LLC.

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We report a novel method termed matrix suppressed laser desorption/ionization to improve the analysis of low-mass molecules by MALDI-TOF mass spectrometry. In this method, the surfactant of cetrimonium bromide (CTAB) is added to the conventional matrix of alpha-cyano-4-hydroxycinnamic acid solution to prepare the MALDI samples. During the MALDI process, the presence of CTAB could substantially or even completely suppress the matrix-related ion background. As a result, very clean mass spectra can be routinely obtained in the low-mass range. In addition, the presence of CTAB can significantly improve the mass resolution of low-mass molecules. It is seen that high-quality spectra were routinely obtained at a matrix/CTAB ratio of 1000:1. This method has been successfully used to analyze a variety of low-mass molecules.

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We have examined interactions between mitoxantrone (MXT) and DNA duplexes or triplexes with different base compositions by using electrospray ionization mass spectrometry (ESI-MS), respectively. MXT interacts preferentially with DNA duplexes compared to the triplexes. In the mass spectrum of the duplex-MXT mixture, the complex peaks dominated in the ratios of duplex/MXT of 1:1, 1:2 and 1:3, and the 1:2 duplex/MXT peak was the most abundant. In contrast, only 1:1 triplex-MXT complexes were observed in the mass spectrum of the triplex-MXT mixture, and the most intensive peak was a free triplex ion without MXT.

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A simple and high-throughput method for the identification of disulfide-containing peptides utilizing peptide-matrix adducts is described. Some commonly used matrices in MALDI mass spectrometry were found to specifically react with sulfhydryl groups within peptide, thus allowing the observation of the peptide-matrix adduct ion [M + n + n' matrix + H](+) or [M + n + n' matrix + Na](+) (n = the number of cysteine residues, n' = 1, 2, ..., n) in MALDI mass spectra after chemical reduction of disulfide-linked peptides. Among several matrices tested, alpha-cyano-4-hydroxycinnamic acid (CHCA, molecular mass 189 Da) and alpha-cyano-3-hydroxycinnamic acid (3-HCCA) were found to be more effective for MALDI analysis of disulfide-containing peptides/proteins. Two reduced cysteines involved in a disulfide bridge resulted in a mass shift of 189 Da per cysteine, so the number of disulfide bonds could then be determined, while for the other matrices (sinapinic acid, ferulic acid, and caffeic acid), a similar addition reaction could not occur unless the reaction was carried out under alkaline conditions. The underlying mechanism of the reaction of the matrix addition at sulfhydryl groups is proposed, and several factors that might affect the formation of the peptide-matrix adducts were investigated.

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The underivatized saponins from Tribulus terrestris and Panax ginseng have been investigated by electrospray ionization multi-stage tandem mass spectrometry (ESI-MSn). In ESI-MS spectra, a predominant [M + Na](+) ion in positive mode and [M - H](-) ion in negative mode were observed for molecular mass information. Multi-stage tandem mass spectrometry of the molecular ions was used for detailed structural analysis. Fragment ions from glycoside cleavage can provide information on the mass of aglycone and the primary sequence and branching of oligosaccharide chains in terms of classes of monosaccharides. Fragment ions from cross-ring cleavages of sugar residues can give some information about the linkages between sugar residues. It was found that different alkali metal-cationized adducts with saponins have different degrees of fragmentation, which may originate from the different affinity of a saponin with each alkali metal in the gas phase. ESI-MSn has been proven to be an effective tool for rapid determination of native saponins in extract mixtures, thus avoiding tedious derivatization and separation steps.