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Showing 1–3 of 3 results
Advanced filters: Author: Alvaro Alonso-Caballero Clear advanced filters

  • Bacteria use thioester-bond-containing proteins to covalently bind to host surfaces and withstand large mechanical shocks. Now, thioester bond reactivity has been shown to be force-dependent: forces >35 pN inhibit bond cleavage by primary amine ligands, whereas forces <6 pN enable reversible reformation. This force-modulated thioester bond reactivity could potentially enable bacterial mobility and a route by which they optimize infection.

    • Alvaro Alonso-Caballero
    • Daniel J. Echelman
    • Julio M. Fernandez
    Research
    Nature Chemistry
    Volume: 13, P: 172-181

  • The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show that the oxidoreductase DsbA also acts as a folding chaperone on the domains.

    • Alvaro Alonso-Caballero
    • Jörg Schönfelder
    • Raul Perez-Jimenez
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11

  • Single-molecule spectroscopy analyses of titin fragments from modern animals and reconstructed from the last common ancestors to mammals, sauropsids and tetrapods shed light on the evolution of the mechanical properties of muscle titin from the Paleozoic to our days.

    • Aitor Manteca
    • Jörg Schönfelder
    • Raul Perez-Jimenez
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 652-657