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P. G. Gucciardi,R. Micheletto,M. Allegrini,T. Kotani,T. Hatada,Y. Kawakami 한국물리학회 2005 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.47 No.1
Distributed Bragg Reflectors (DBRs) have been found to be very effective in increasing the efficiency of light emitting diodes and semiconductor laser devices. By using polarization-modulated scanning near-field optical microscopy (PM-SNOM), we investigate the optical response to different illumination polarization states of a DBR structure that consists of a stack of quarter wavelength thick slabs of dielectrics with alternating high and low refractive index. The DBR has been optically characterized in the near-field at different wavelengths in illumination- and in collection- mode with light excitation orthogonal to the probe axis, for fixed as well as for modulated polarization. We have found that the optical signal does not follow the morphological structure of the slabs, as expected but it shows a different spatial periodicity related to the excitation properties and to the interplay of the different DBR planes.
P. G. Gucciardi,A. Favaloro,A. Pisani,G. Cutroneo,P. Princi 한국물리학회 2005 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.47 No.1
The -Sarcoglycan and the f-actin are two protein systems with structural and signaling functions, allowing interaction between muscle fibers and extra cellular matrix. Although numerous studies have been conducted on these systems, their localization and distribution patterns along the nonjunctional sarcolemma are not clear. In this paper we first apply fluorescence Near-Field Optical Microscopy to study this problem on human muscle cells, taking advantage of the enhanced spatial resolution of this technique. Samples of human muscle (vastus lateralis) are analyzed, obtained during orthopedic surgery from subjects not affected by neuromuscular diseases. Following the protocol used to carry out indirect immunofluorescence, TRITC-conjugated IgG anti-mouse in goat has been used as the first fluorochrome and, after saturation of residual free binding sites, sections have been incubated with a second antibody conjugated with FITC fluorochrome. Samples, first studied by fluorescence confocal microscopy, show that all tested proteins have a localized,periodic (costameric) spatial distribution. Subsequent SNOM studies have been aimed both to the single localization of the proteins along the cell membrane, and to the double localization of the proteins with respect to each other. The typical costameric band structure has been evidenced in both the fluorescence and the topography maps of dry cells, with a period of 2 μm for both proteins. A careful correlation between the opography (not available in confocal microscopy) and the fluorescence information permits to draw conclusions on the spatial localization of the two proteins, confirming the results found in confocal microscopy.