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  • 1
    Electronic Resource
    Electronic Resource
    Natural language interface for an expert system (1998)
    Oxford, UK and Boston, USA : Blackwell Publishers Ltd
    Expert systems 15 (1998), S. 0 
    Details
    ISSN: 1468-0394
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Computer Science
    Notes: This paper provides complete analysis of natural language interface from the screen manager to the parser/understander, even though it has some limitations. The main focus is on the design and development of a subsystem for understanding natural language input in an expert system. Fast response time and user-friendliness were the most important considerations in the design. The screen manager provides an easy editing capability for the user. The spelling correction system can detect most spelling errors and correct them automatically, quickly and effectively. The Lexical Functional Grammar (LFG) parser and the understander are designed to handle most types of simple sentences, fragments, and ellipses. As a result, this system as applied to a man-machine dialogue gives improved ill-formed natural language input handling capabilities to the expert system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/1468-0394.00080
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A magnesium(II) complex of 1,10-phenanthroline-2,9-dicarboxylate (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. m154-m156 
    Details
    ISSN: 1600-5368
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The title compound, triaqua(1,10-phenanthroline-2,9-dicarboxylato)magnesium(II) dihydrate, [Mg(PDA)(H2O)3]·2H2O, (H2PDA is 1,10-phenanthroline-2,9-dicarboxylic acid, C14H8N2O4) has twofold crystallographic symmetry. The Mg atom is in a distorted pentagonal bipyramidal coordination environment with two N atoms and two O atoms from PDA and one O atom from a water molecule forming the pentagonal plane, and two O atoms from two water molecules occupying axial positions. The crystal structure comprises an infinite two-dimensional network of hydrogen-bonded molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S1600536801004317
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning, expression and characterization of l-arabinose isomerase from Thermotoga neapolitana: bioconversion of d-galactose to d-tagatose using the enzyme (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 212 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Gene araA encoding an l-arabinose isomerase (AraA) from the hyperthermophile, Thermotoga neapolitana 5068 was cloned, sequenced, and expressed in Escherichia coli. The gene encoded a polypeptide of 496 residues with a calculated molecular mass of 56 677 Da. The deduced amino acid sequence has 94.8% identical amino acids compared with the residues in a putative l-arabinose isomerase of Thermotoga maritima. The recombinant enzyme expressed in E. coli was purified to homogeneity by heat treatment, ion exchange chromatography and gel filtration. The thermophilic enzyme had a maximum activity of l-arabinose isomerization and d-galactose isomerization at 85°C, and required divalent cations such as Co2+ and Mn2+ for its activity and thermostability. The apparent Km values of the enzyme for l-arabinose and d-galactose were 116 mM (vmax, 119 μmol min−1 mg−1) and 250 mM (vmax, 14.3 μmol min−1 mg−1), respectively, that were determined in the presence of both 1 mM Co2+ and 1 mM Mn2+. A 68% conversion of d-galactose to d-tagatose was obtained using the recombinant enzyme at the isomerization temperature of 80°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11254.x
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    Paper (German National Licenses)
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