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  • American Institute of Physics (AIP)  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 83 (1998), S. 480-485 
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A reflectance anisotropy spectroscopy (RAS) and low-energy electron diffraction study of the InP(001) surface is presented. The surface was prepared by thermal desorption of an As-P capped epilayer grown by molecular beam epitaxy. RA spectra have been monitored over a spectral range of 1.5–5.5 eV at regular intervals during thermal decapping and annealing up to the point of decomposition (553–973 K). Each of the RA spectra of the surface reconstructions comprise positive (at 2.9 eV) and negative (at 1.8 eV) anisotropies which have been previously associated with P- and In-related bonding, respectively. Unlike other III-V (001) semiconductor surfaces, the evolution of different reconstructions cannot be explained in terms of a change in surface stoichiometry which involves loss of the anion species. In the case of InP(001) the P species contributes to the clean surface reconstruction from the early stages of decapping to the point of decomposition. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 43 (1998), S. 89-98 
    ISSN: 0021-9304
    Keywords: gelatin ; films ; tissue ; bonding ; argon beam ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Cross-linked gelatin films were bonded to heart muscle and to lung pleura and parenchyma using the electrical discharge of an argon beam radiofrequency coagulator. The bonds were stable in warm saline buffer for minutes to hours. Bonding was thought to partly occur through a mechanical interlock of film and tissue elements. The interdigitation of tissue and film arose during exposure to the argon beam, which denatured protein constituents of both, and created a fluidized state that rapidly coalesced. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res (Appl Biomater) 43: 89-98, 1998
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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