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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 2 (1993), S. 313-318 
    ISSN: 1057-9257
    Keywords: MOCVD ; MAS-NMR ; CARS ; Quantum effects ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Coherent anti-Stokes Raman scattering (CARS) has been utilised to monitor the decomposition of trimethylgallium (TMGa) on the reactive internal surface of the protonated form of zeolite Y under metal organic chemical vapour deposition (MOCVD) conditions designed to produce GaP deposits that exhibit quantum-size effects. The CARS data clearly reveal the facile room temperature decomposition of TMGa in the zeolite, as evidenced by the detection of increasing levels of methane with increasing reaction time. In addition, the zeolite samples were analysed by solid state nuclear magnetic resonance with magic angle spinning (MAS NMR) before reaction, after reaction of TMGa and after subsequent reaction with phosphine at 300°C. These data reveal that TMGa reacts with acid sites in the zeolite 12-rings, resulting in species containing methyl groups. Subsequent exposure to phosphine removes these methyl group protons, leaving various, as yet not fully characterised, phosphorus species. Exposure to phosphine does not appear to regenerate the acid sites on the zeolite.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Computational Chemistry 15 (1994), S. 61-71 
    ISSN: 0192-8651
    Keywords: Computational Chemistry and Molecular Modeling ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Computer Science
    Notes: Zinc ions have been shown to inhibit human immunodeficiency virus type 1 (HIV-1) protease in vitro at neutral pH [Zhang et al. Biochemistry, 36, 8717 (1991)]. Kinetic data from this study support a reversible binding mechanism of zinc in the active site. Preliminary calculations of the ion-protein potential energy based on the geometry of the crystallographic structure [Wlodawer et al. Science, 245, 616 (1989)] are consistent with this proposed mechanism. To examine the structure of HIV-1 protease with zinc bound in the active site, molecular dynamics simulations in the presence and absence of zinc at this site have been carried out to 200 ps. These simulations suggest zinc remains stably bound to the catalytic aspartate residues without disruption of the dimer or significant alteration of the active site structure. These data are consistent with those observed by Zhang et al. (1991), and together give strong evidence that this is the binding site that leads to inactivation. A proposed model of zinc binding at the active site based on quantum mechanical calculations indicates Zn+2 coordination is monodentate with each catalytic aspartate, leaving at least two ligand positions potentially free (occupied by water molecules in the calculations). © 1994 by John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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