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Literature summary for 3.2.1.17 extracted from

  • Frare, E.; Mossuto, M.F.; de Laureto, P.P.; Tolin, S.; Menzer, L.; Dumoulin, M.; Dobson, C.M.; Fontana, A.
    Characterization of oligomeric species on the aggregation pathway of human lysozyme (2009), J. Mol. Biol., 387, 17-27.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Renatured (Commentary)

Renatured (Comment) Organism
characterization of oligomers obtained after 5 days incubation at pH 3.0 and 60°C. Oligomers are misfolded species when compared to monomeric lysozyme, with a prevalence of random structure but with significant elements of the beta-sheet structure that is characteristic of the mature fibrils. The oligomeric lysozyme aggregates are more susceptible to proteolysis with pepsin than both the monomeric protein and the mature fibrils Homo sapiens