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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    ISSN: 0887-3585
    Keywords: peptide folding ; disulfide framework ; insect toxins ; NMR ; distance geometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: An analysis of the sequences of scyllatoxin and charybdotoxin suggested that it would be possible to design a core peptide sequence which would still fold to give the β-hairpin and helix seen in the toxins, but which would eliminate one disulfide and connecting residues. The core sequence was modeled, then synthesized and purified. The cysteines oxidize in air to give the same disulfide pairings as seen in the parent toxins as the major product. The three-dimensional structure of the core sequence peptide, termed Max, was determined using proton NMR spectroscopy and found to be identical in secondary structure to the toxins. However differences were found in the relative orientation of the β-hairpin and helix. The use of this structural motif, found in many insect toxins, as a disulfide framework for exploring sequence/structure/activity relationships is discussed. © 1994 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 2
    London : Henry Stewart Talks
    Keywords: Evolution ; Medicine
    Description / Table of Contents: Contents: Arms races and evolutionary arms races -- What are they and how are they defined -- Features of arms races -- Who wins?: the Red Queen and the life-dinner principle -- Common arms races in nature -- Predators and prey, sexual selection, parent offspring conflict and host-parasite coevolution -- HIV evolution, parent-infant resemblance in humans and genomic imprinting
    Notes: Animated audio-visual presentation with synchronized narration.
    Pages: 1 streaming video file (39 min.) : digital, mono., SWF file, sd., col.
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