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Showing 1–17 of 17 results
Advanced filters: Author: Sergi Garcia-Manyes Clear advanced filters

  • The dynamics of a complex chemical reaction that occurs through a well-defined intermediate have been followed at the single-molecule level using a 'nanoreactor' set-up, revealing a primary hydrogen isotope effect that is invisible to ensemble experiments.

    • Sergi Garcia-Manyes
    News & Views
    Nature Chemistry
    Volume: 2, P: 905-906

  • Mechanical forces can be used as an alternative source of energy to increase chemical reactivity. This Review reports on the latest single-molecule measurements and how they have improved the current understanding of single-bond mechanochemistry.

    • Sergi Garcia-Manyes
    • Amy E. M. Beedle
    Reviews
    Nature Reviews Chemistry
    Volume: 1, P: 1-16

  • Post-translational modifications modulate nanomechanics of proteins. Here the authors use single-molecule force-clamp spectroscopy supported by density functional theory calculations to show how reactive low-weight molecular thiol compounds directly affect mechanical protein folding.

    • Amy E. M. Beedle
    • Marc Mora
    • Sergi Garcia-Manyes
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • In metalloproteins, a metal cofactor participates in the formation of the correct fold. Here the authors demonstrate—using single molecule force spectroscopy and the native copper centre as an embedded internal reporter—that the blue-copper proteins azurin and plastocyanin unfold via two independent competing pathways under force.

    • Amy E. M. Beedle
    • Ainhoa Lezamiz
    • Sergi Garcia-Manyes
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-9

  • Mechanical force can facilitate thermodynamically unfavourable reactions. Here, the authors found that a stretching force can promote the SN2 cleavage of a protein disulfide bond by weak nucleophilic thiols, and that removing this force reverses the reaction yielding the original disulfide bond.

    • Amy E. M. Beedle
    • Marc Mora
    • Sergi Garcia-Manyes
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-9

  • Mechanical stretching of a protein can be studied in detail using single-molecule experiments, and is shown to have an accelerating effect on its reaction with a nucleophile. The observation of a dramatic switch in the effect above a threshold force suggests an abrupt change in protein conformation and a change in reaction mechanism.

    • Sergi Garcia-Manyes
    • Jian Liang
    • Julio M. Fernández
    Research
    Nature Chemistry
    Volume: 1, P: 236-242

  • 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

  • Electro-osmosis in an anion-selective α-hemolysin nanopore is used to capture, unfold and transport polypeptides of over 1,200 residues, which allows the mapping of post-translational modifications in polypeptide chains by monitoring the ionic current at a single-molecule resolution.

    • Pablo Martin-Baniandres
    • Wei-Hsuan Lan
    • Hagan Bayley
    ResearchOpen Access
    Nature Nanotechnology
    Volume: 18, P: 1335-1340

  • Using phylogenetic analysis, ancestral forms of thioredoxin reflecting the sequences likely to have existed at key evolutionary points have now been synthesized and analyzed. Single-molecule analysis indicates that all of the reconstructed enzymes use the extant reaction mechanism but that the most ancient are optimally active at low pH and resistant to higher temperatures, conditions that would have existed on early earth.

    • Raul Perez-Jimenez
    • Alvaro Inglés-Prieto
    • Julio M Fernandez
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 592-596

  • Mechanical force modulates the conformation and function of individual proteins, and this underpins many mechanically driven cellular processes. This Review addresses single-molecule force spectroscopy experiments conducted on proteins with a known role in mechanosensing and mechanotransduction in eukaryotic cells.

    • Amy E. M. Beedle
    • Sergi Garcia-Manyes
    Reviews
    Nature Reviews Materials
    Volume: 8, P: 10-24