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  • American Association for the Advancement of Science (AAAS)  (1)
  • Royal Society  (1)
  • 1
    Publication Date: 2018-07-26
    Description: Composite superhydrophobic coating built with film former and filler is attracting much attention for its facile and convenient fabrication, but significant limitations and disadvantages still remain. In this paper, a composite superhydrophobic coating is introduced which can be cured at room temperature and made by dispersing modified silica nanoparticles with 1H, 1H, 2H, 2H-perfluorooctyltriethoxysilane in fluorosilicone resin. Silica content and dispersion time showed obvious influences on the morphology and topography of composite coating by reuniting dispersed nanoparticles to form peaks on the surface. Excessively large distances between these peaks would decrease water contact angle value. Increasing slope of peaks, appropriate distance between peaks and decreasing diameter size of peaks would diminish sliding angle value. Formation mechanism of the composite coating based on fluorosilicone resin and modified nanoparticles was explained using interpenetrating polymer model.
    Keywords: materials science
    Electronic ISSN: 2054-5703
    Topics: Natural Sciences in General
    Published by Royal Society
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  • 2
    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2018-08-10
    Description: The Hedgehog (Hh) pathway involved in development and regeneration is activated by the extracellular binding of Hh to the membrane receptor Patched (Ptch). We report the structures of human Ptch1 alone and in complex with the N-terminal domain of human Sonic hedgehog (ShhN) at resolutions of 3.9 and 3.6 angstroms, respectively, as determined by cryo–electron microscopy. Ptch1 comprises two interacting extracellular domains, ECD1 and ECD2, and 12 transmembrane segments (TMs), with TMs 2 to 6 constituting the sterol-sensing domain (SSD). Two steroid-shaped densities are resolved in both structures, one enclosed by ECD1/2 and the other in the membrane-facing cavity of the SSD. Structure-guided mutational analysis shows that interaction between ShhN and Ptch1 is steroid-dependent. The structure of a steroid binding–deficient Ptch1 mutant displays pronounced conformational rearrangements.
    Keywords: Biochemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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