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  • 1
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 80 (1996), S. 440-447 
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The origin and interpretation of the Raman features of amorphous (hydrogenated) carbon films deposited at room temperature in the region of 1000–1700 cm−1 is discussed in this paper. Possible interpretations of the linewidths, positions of the "G'' graphite peak and "D'' disordered peak, and their intensity ratios are examined using results obtained from magnetron sputtered and magnetic field enhanced plasma deposited films. It is shown that even small "clusters'' of condensed benzene rings (cluster size below 20 A(ring)) in carbon films can explain the observed Raman scattering. Besides the care that should be taken in the correct interpretation of Raman results, the utility of Raman scattering in obtaining an estimate of cluster sizes in amorphous (hydrogenated) carbon films is discussed. Carbon films prepared by magnetron sputtering show two additional Raman features at 1180 and 1490 cm−1 in addition to the G and D peaks. It is shown that a correlation exists between the 1180 cm−1 peak and the sp3 content in the films. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 84 (1998), S. 2071-2081 
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Nitrogenated and hydrogenated amorphous carbon (a-C:H:N) films have been deposited by a plasma beam source using a gas mixture of C2H2, Ar and N2. The Ar/C2H2 ratio is kept constant at a ratio of 3, with the nitrogen flow allowed to vary. Nonnitrogenated films, with Ar/C2H2 ratios of 3 and 6 were also deposited and analyzed before attempting to identify the modifications to the microstructural properties due to nitrogen doping. The nitrogenated and hydrogenated a-C (a-C:H:N) films deposited in this study reveal interesting properties with regard to their optical gap, electrical conductivity, and mobility of the charge carriers. The optical E04 gap passes through a maximum of 2.7 eV as a function of incorporated nitrogen. The electrical conductivity, too, reaches a peak value of 10−3(Ω cm)−1 with increasing optical gap and remains constant for higher N2 flows. The electrical conductivity process is thermally activated with activation energies in the range 0.1–0.3 eV. This is discussed in terms of the mobility of the charge carriers (determined by Hall measurements) and electronic doping. The defect density (measured by electron spin resonance) is found to decrease with increasing nitrogen incorporation. The films have also been characterized by infrared spectroscopy, photo thermal deflection, and Raman spectroscopy. The microstructure of the deposited a-C:H:N films is discussed in terms of the electronic density of states. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The cysteine protease Der p1 from dust mite of the genus Dermatophagoides pteronyssinus is a major type I allergen. About 80% of house dust mite (HDM) allergic individuals are reactive to this protease in standard assays for detection of IgE. A curative treatment for atopic allergy is immunotherapy (IT) with HDM extracts which are complex mixtures occasionally resulting in anaphylactic reactions. Novozymes focuses on developing a recombinant variant of Der p1 which exhibit lowered risk of IgE-mediated allergic reactions, while maintaining its ability to trigger proper Th-cell responses. This may provide a safer alternative for specific IT of HDM allergy. A secreted recombinant form of pro-Der p 1 expressed by Saccharamyces cerevisiae was obtained by fusion of the pro-enzyme to a fungal signal peptide. The N-glycosylation site of Der p1 was mutated resulting in a deglycosylated pro-enzyme with a molecular mass of 35 kDa. Protein purification procedure was developed to obtain nearly pure Der p1 protein followed by determination of concentration by active-site-titration with the cysteine protease inhibitor E64. The deglycosylated recombinant pro-Der p 1 revealed immunologic similarity to the native Der p 1 molecule when compared in basophile histamine release, IgE-binding assays and T-cell proliferation assays. By in silico epitope mapping of a modelled 3-dimensional structure of Der p1, five putative IgG and IgE epitopes were predicted. By protein engineering, the predicted epitopes were removed one by one in Der p1 and screening for hypoallergenic variants was performed.
    Type of Medium: Electronic Resource
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