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Showing 1–8 of 8 results
Advanced filters: Author: Rafael Tapia-Rojo Clear advanced filters

  • Vinculin binding to talin is a key event in focal adhesion dynamics; yet, how vinculin is activated to recruit actin remains unknown. Here, the authors use a multiscale approach to reveal that talin activates vinculin through an intricate allosteric mechanism tightly regulated by force.

    • Florian Franz
    • Rafael Tapia-Rojo
    • Frauke Gräter
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-16

  • Proteins fold under mechanical force during co-translational folding at the ribosome. Here, the authors use single molecule magnetic tweezers to study the influence of chaperones on protein folding and show that the ribosomal chaperone trigger factor acts as a mechanical foldase by promoting protein folding under force.

    • Shubhasis Haldar
    • Rafael Tapia-Rojo
    • Julio M. Fernandez
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-7

  • Testing mechanical forces on native molecules in natural environments remains a challenge. Here the authors engineer titin to carry a HaloTag-TEV insertion to allow analysis of dynamics under force in muscle fibers.

    • Jaime Andrés Rivas-Pardo
    • Yong Li
    • Jorge Alegre-Cebollada
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • 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