924 resultados para Loss mass analysis
Resumo:
In this paper, the use of magnetic materials to divert flux in high-temperature superconductor superconducting coils and reduce transport ac loss is investigated. This particular technique is preferred over other techniques, such as striation, Roebel transposition, and twisted wires because it does not require modification to the conductor itself, which can be detrimental to the properties of the superconductor. The technique can also be implemented for existing coils. The analysis is carried out using a coil model based on the H formulation and implemented in comsol multiphysics. Both weakly and strongly magnetic materials are investigated, and it is shown that the use of such materials can divert flux and achieve a reduction in transport ac loss, which, in some cases, is quite significant. This analysis acts to provide a foundation for further optimization and experimental work in the future. © 2011 IEEE.
Resumo:
The ion-exchange equilibrium of bovine serum albumin (BSA) to an anion exchanger, DEAE Spherodex M, has been studied by batch adsorption experiments at pH values ranging from 5.26 to 7.6 and ionic strengths from 10 to 117.1 mmol/l. Using the unadjustable adsorption equilibrium parameters obtained from batch experiments, the applicability of the steric mass-action (SMA) model was analyzed for describing protein ion-exchange equilibrium in different buffer systems. The parametric sensitivity analysis was performed by perturbing each of the model parameters, while holding the rest constant. The simulation results showed that, at high salt concentrations or low pHs close to the isoelectric point of the protein, the precision of the model prediction decreased. Parametric sensitivity analysis showed that the characteristic charge and protein steric factor had the largest effects on ion-exchange equilibrium, while the effect of equilibrium constant was about 70%-95% smaller than those of characteristic charge and steric factor under all conditions investigated. The SMA model with the relationship between the adjusted characteristic charge and the salt concentration can well predict the protein adsorption isotherms in a wide pH range from 5.84 to 7.6. It is considered that the SMA model could be further improved by taking into account the effect of salt concentration on the intermolecular interactions of proteins. (c) 2006 Elsevier Ltd. All rights reserved.
Resumo:
The guided modes of a two-dimensional photonic crystal straight waveguide and a waveguide bend are studied in order to find the high transmission mechanism for the waveguide bend. We find that high transmission occurs when the mode patterns and wave numbers match, while the single-mode condition in the waveguide bend is not necessarily required. According to the mechanism, a simply modified bend structure with broad high transmission band is proposed. The bandwidth is significantly increased from 19 to 116 nm with transmission above 90%, and covers the entire C band of optical communication.
Resumo:
Charged-particle spectra associated with direct photon (gamma(dir)) and pi(0) are measured in p + p and Au + Au collisions at center-of-mass energy root(S)(NN) = 200 GeV with the STAR detector at the Relativistic Heavy Ion Collider. A shower-shape analysis is used to partially discriminate between gamma(dir) and pi(0). Assuming no associated charged particles in the gamma(dir) direction ( near side) and small contribution from fragmentation photons (gamma(frag)), the associated charged-particle yields opposite to gamma(dir) (away side) are extracted. In central Au + Au collisions, the charged-particle yields at midrapidity (vertical bar eta vertical bar < 1) and high transverse momentum (3 < (assoc)(PT) < 16 GeV/c) associated with gamma(dir) and pi(0) (vertical bar eta vertical bar < 0.9, 8 < (trig)(PT) < 16 GeV/c) are suppressed by a factor of 3-5 compared with p + p collisions. The observed suppression of the associated charged particles is similar for gamma(dir) and pi(0) and independent of the gamma(dir) energy within uncertainties. These measurements indicate that, in the kinematic range covered and within our current experimental uncertainties, the parton energy loss shows no sensitivity to the parton initial energy, path length, or color charge.
Resumo:
Pressurized capillary electrochromatography (pCEC) was coupled with electrospray ionization mass spectrometry (ESI-MS) using a coaxial sheath liquid interface. It was used for separation and analysis of peptides and proteins. The effects of organic modifier and applied voltage on separation were investigated, and the effects of pH value of the mobile phase and the concentration of the electrolyte on ESI-MS signal were investigated. The resolution and detection sensitivity with different separation methods (pCEC, capillary high-performance liquid chromatography) coupled on-line with mass spectrometry were compared for the separation of a peptide mixture. To evaluate the feasibility and reliability of the experimental setup of the system, tryptic digests of cytochrome c and modified protein as real samples were analyzed by using pCEC-ESI-MS.
Resumo:
Low temperature heat capacities of N-(p-methylphenyl)-N'-(2-pyridyl)urea were determined by adiabatic calorimetry method in the temperature range from 80 to 370 K. It was found that there was not any heat anomaly in this temperature region. Based on the experimental data, some thermodynamic function results were obtained. Thermal stability and decomposition characteristics analysis of N-(p-methylphenyl)-N'-(2-pyridyl)urea were carried out by DSC and TG. The results indicated that N-(p-methylphenyl)-N'-(2-pyridyl)urea started to melt at ca. 426 K (153degreesC) and the melting peak located at 447.01 K (173.86degreesC). The melting enthalpy was 204.445 kJ mol(-1) (899.6 J g(-1)). The decomposition peak of N-(p-methylphenyl)-N'-(2-pyridyl)urea was found at 499.26 K (226.11degreesC) from DSC curve. This result was similar with that from TG and DTG experiment, in which the mass loss peak was determined as 500.4 K (227.2degreesC).
Resumo:
Since protein phosphorylation is a dominant mechanism of information transfer in cells, there is a great need for methods capable of accurately elucidating sites of phosphorylation. In recent years mass spectrometry has become an increasingly viable alternative to more traditional methods of phosphorylation analysis. The present study used immobilized metal affinity chromatography (IMAC coupled with a linear ion trap mass spectrometer to analyze phosphorylated proteins in mouse liver. A total of 26 peptide sequences defining 26 sites of phosphorylation were determined. Although this number of identified phosphoproteins is not large, the approach is still of interest because a series of conservative criteria were adopted in data analysis. We note that, although the binding of non-phosphorylated peptides to the IMAC column was apparent, the improvements in high-speed scanning and quality of MS/MS spectra provided by the linear ion trap contributed to the phosphoprotein identification. Further analysis demonstrated that MS/MS/MS analysis was necessary to exclude the false-positive matches resulting from the MS/MS experiments, especially for multiphosphorylated peptides. The use of the linear ion trap considerably enabled exploitation of nanoflow-HPLC/MS/MS, and in addition MS/MS/MS has great potential in phosphoproteome research of relatively complex samples. Copyright (C) 2004 John Wiley Sons, Ltd.