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  • biophysicsX-ray solution scatteringphotocagingstructural biology  (1)
  • electronic materialswide band gap materialssemiconductorssilicongermanium  (1)
  • International Union of Crystallography (IUCr)  (2)
  • 2015-2019  (2)
  • 1995-1999
  • 1970-1974
  • 1935-1939
Collection
Publisher
  • International Union of Crystallography (IUCr)  (2)
Years
  • 2015-2019  (2)
  • 1995-1999
  • 1970-1974
  • 1935-1939
Year
  • 1
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    International Union of Crystallography (IUCr)
    In: IUCrJ
    Publication Date: 2015-08-16
    Description: The development of semiconductor electronics is reviewed briefly, beginning with the development of germanium devices (band gap Eg = 0.66 eV) after World War II. A tendency towards alternative materials with wider band gaps quickly became apparent, starting with silicon (Eg = 1.12 eV). This improved the signal-to-noise ratio for classical electronic applications. Both semiconductors have a tetrahedral coordination, and by isoelectronic alternative replacement of Ge or Si with carbon or various anions and cations, other semiconductors with wider Eg were obtained. These are transparent to visible light and belong to the group of wide band gap semiconductors. Nowadays, some nitrides, especially GaN and AlN, are the most important materials for optical emission in the ultraviolet and blue regions. Oxide crystals, such as ZnO and β-Ga2O3, offer similarly good electronic properties but still suffer from significant difficulties in obtaining stable and technologically adequate p-type conductivity.
    Keywords: electronic materialswide band gap materialssemiconductorssilicongermanium
    Electronic ISSN: 2052-2525
    Topics: Geosciences , Physics
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  • 2
    Publication Date: 2018-09-13
    Description: This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecules allow the observation of single-turnover reactions of non-naturally photoactivatable proteins. The kinetics of the reaction can be derived from changes in X-ray scattering associated with ATP-binding and subsequent dimerization. This method can be expanded to any small-molecule-driven protein reaction with conformational changes traceable by X-ray scattering where the small molecule can be photocaged.
    Keywords: biophysicsX-ray solution scatteringphotocagingstructural biology
    Electronic ISSN: 2052-2525
    Topics: Geosciences , Physics
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