221 resultados para MATRIX-ENSEMBLES


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Structural dependence on annealing of a-SiOx:H was studied by using infrared absorption and Raman scattering. The appearance of Raman peaks in the range of 513-519cm(-1) after 1170 degreesC annealing was interpreted as the formation nanocrystalline silicon with the sizes from 3-10nm. The Raman spectra also show the existence of amorphous-like silicon phase, which is associated with Si-Si bond re-construction at boundaries of silicon nanocrystallites. The presence of the shoulder at 980cm(-1) of Si-O-Si stretching vibration at 1085cm(-1) in infrared spectra imply that except that SiO2 phase, there is silicon sub-oxide phase in the films annealed at 1170 degreesC. This sub-oxide phase is located at the interface between Si crystallites and SiO2, and thus support the shell model for the mixed structures of Si grains and SiO2 matrix.

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We investigate the annealing behavior of Photoluminescence (PL) from self-assembled InAs quantum dots (QDs) with different thicknesses GaAs cap layers. The diffusion introduced by annealing treatment results in a blue-shift of the QD PL peak, and a decrease in the integrated intensity. The strain present in QDs enhances the diffusion, and the QDs with the cap layers of different thicknesses will experience a strain of different strength. This can lend to a, better understanding of the larger blue-shift of the PL peak of the deeper buried QDs, and the different variance of the full width at half maximum of the luminescence from QDs with the cap layers of different thicknesses.

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The steplike density of states obtained from reflectance-difference spectroscopy demonstrates that ultrathin InAs layers should be regarded as two-dimensional quantum wells rather than isolated clusters, even for the sample with only 1/3 monolayer InAs in (311)-oriented GaAs. The degree of anisotropy is within the intrinsic anisotropy of (311)-oriented ultrathin quantum wells, indicating that there is little structural or strain anisotropy in the InAs islands. (C) 1998 Elsevier Science B.V.

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We calculate the in-medium nucleon-nucleon scattering cross sections from the G-matrix using the Dirac-Brueckner-Hartree-Fock (DBHF) approach. And we investigate the influence of the different representations of the G-matrix to the cross sections, the difference of which is mainly from the different effective masses.

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The isoflavonoids in Radix astragali were determined and identified by HPLC-photodiode array detection-MS after extraction employing matrix solid-phase dispersion (MSPD). As a new sample preparation method for R. astragali, the MSPD procedure was optimized, validated and compared with conventional methods including ultrasonic and Soxhlet extraction. The amounts of two major components in this herb, formononetin (6) and ononin (2), were determined based on their authentic standards. Four major isoflavonoids, formononetin (6), ononin (2), calycosin (5) and its glycoside (1), and three minor isoflavonoids, (6aR,11aR)-3-hydroxy-9, 10-dimethoxypterocarpan (7), its glycoside (3), and (3R)-7,2'-dihydroxy-3',4'-dimethoxyisoflavone-7-O-beta-D-glycoside (4), were identified based on their characteristic two-band UV spectra and [M + H](+), [aglycone + H](+) and [A1 + H](+) ions, etc. The combined MSPD and HPLC-DAD-MS method was suitable for quantitative and qualitative determination of the isoflavonoids in R. astragali. (C) 2003 Elsevier B.V. All rights reserved.

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Desorption/ionization on silicon mass spectrometry (DIOS-MS) is a matrix-free technique that allows for the direct desorption/ionization of low-molecular-weight compounds with little or no fragmentation of analytes. This technique has a relatively high tolerance for contaminants commonly found in biological samples. DIOS-MS has been applied to determine the activity of immobilized enzymes on the porous silicon surface. Enzyme activities were also monitored with the addition of a competitive inhibitor in the substrate solution. It is demonstrated that this method can be applied to the screening of enzyme inhibitors. Furthermore, a method for peptide mapping analysis by in situ digestion of proteins on the porous silicon surface modified by trypsin, combined with matrix-assisted laser desorption/ionization-time of flight-MS has been developed.

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A novel protocol has been established to separate dsDNA fragments with high efficiency on glass chips by using an ultralow viscosity sieving matrix with added glucose. Low-molecular-weight hydroxypropylmethylcellulose (HPMC), with a viscosity nearly equivalent to that of water, was used to electrophoretically separate fluorescent inter-calator-labeled double-stranded DNA (dsDNA) fragments on microfluidic glass chips. In comparison with conventional sieving protocols, low-molecular-weight HPMC as sieving matrix could result in reduced running cost and analysis time, in addition to a comparable separation efficiency of dsDNA fragments. In this paper, the addition of glucose was investigated to enhance the separation of DNA in the lowest viscosity polymer evaluated. The effect of staining dye and field strength were also evaluated. At an applied electric field strength of 200 V/cm, satisfactory resolution of the PBR322/HaeIII DNA marker could be achieved within 4 min by using 2% HPMC-5 with 6% glucose added. Coelectrophoresing PCR product along with phiX174/HaeIII DNA sizing marker was also demonstrated by using the ultralow viscosity HPMC-5 solution on a glass chip.

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Peptide mass mapping analysis, utilizing a regenerable enzyme microreactor with metal-ion chelated adsorption of enzyme, combined with matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF-MS) was developed. Different procedures from the conventional approaches were adopted to immobilize the chelator onto the silica supports, that is, the metal chelating agent of iminodiacetic acid (IDA) was reacted with glycidoxypropyltrimethoxysilane (GLYMO) before its immobilization onto the inner wall of the fused-silica capillary pretreated with NH4HF2. The metal ion of copper and subsequently enzyme was specifically adsorbed onto the surface to form the immobilized enzyme capillary microreactor, which was combined with MALDI-TOF-MS to apply for the mass mapping analysis of nL amounts of protein samples. The results revealed that the peptide mapping could routinely be generated from 0.5 pmol protein sample in 15 min at 50degreesC, even 20 fmol cytochrome c could be well digested and detected.