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  • 1
    Electronic Resource
    Electronic Resource
    Flexibility of the DNA-binding domains of trp repressor (1988)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 3 (1988), S. 18-31 
    Details
    ISSN: 0887-3585
    Keywords: flexibility ; trp repressor ; DNA-binding domains ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: An orthorhombic crystal form of trp repressor (aporepressor plus L-tryptophan ligand) was solved by molecular replacement, refined to 1.65 Å resolution, and compared to the structure of the repressor in trigonal crystals. Even though these two crystal forms of repressor were grown under identical conditions, the refined structures have distinctly different conformations of the DNA-binding domains. Unlike the repressor/aporepressor structural transition, the conformational shift is not caused by the binding or loss of the L-tryptophan ligand. We conclude that while L-tryptophan binding is essential for forming a specific complex with trp operator DNA, the corepressor ligand does not lock the repressor into a single conformation that is complementary to the operator. This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340030103
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Liposome capillary electrophoresis for analysis of interactions between lipid bilayers and solutes (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1519-1523 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Drug ; Interaction free energy ; Liposome ; Peptide ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Liposomes, which mimic biomembranes, were used as a pseudostationary phase in capillary zone electrophoresis. The decrease in the mobility of an analyte owing to the presence of liposomes reflected interaction between the analyte and the liposomes. Equations were derived to calculate the specific capacity factor Ks (the capacity factor, K′, normalized to the liposome concentration 1 M) from the migration times and to estimate the difference in free energy, Δ(ΔG0), of the weak analyte/liposome interactions. The order of Ks values for the drugs tested was aspirin 〈 salicylic acid 〈 warfarin 〈 sulfasalazine. The peptide TyrGlySerThrProGlyCysCys interacted more strongly with the liposomes (Ks = 10.1 M-1) than did TyrGlySerThrProGlySerSer (Ks = 9.1 M-1). These results were similar to those obtained earlier by immobilized liposome chromatography.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601251
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Syntheses and insecticidal activities of novel 2,5-disubstituted-1,3,4-oxadiazoles (1996)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 67 (1996), S. 124-130 
    Details
    ISSN: 0268-2575
    Keywords: oxadiazole ; organic fluorides ; synthesis ; insecticidal activity ; structure-activity relationship ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A series of novel symmetrical and asymmetrical 2,5-disubstituted-1,3,4-oxadiazoles and their intermediates were synthesized. A convenient procedure for preparation of aromatic nitrile and ester intermediates is reported. The insecticidal activities of oxadiazoles against Dropsophila melanogaster were recorded, and analysis of structure-activity relationships showed that the highest occupied molecular orbital energy (EH) was the main factor to affect the bioactivities.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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