R. Tapia-Rojo

This study identifies an allosteric network in vinculin regulated by talin, showing how force and binding dynamics control focal adhesion formation.

This paper introduces a magnetic tweezers technique to measure single-molecule protein folding dynamics over days, revealing molecular diversity through force response and folding kinetics.

This paper develops a magnetic tweezers method capable of applying high forces with stability and resolution, demonstrating its use on the mechanostable protein FimA.

This study shows talin acts as a mechanical bandpass filter, filtering out noise and detecting periodic force signals through its folding dynamics.

The paper uses magnetic tweezers to observe vinculin-induced contraction of unfolded talin under force, revealing a force-dependent mechanism regulating mechanotransduction in focal adhesions.

The paper introduces a HaloTag-TEV genetic cassette to study protein mechanics in native tissues, showing titin's role in muscle contraction under mechanical forces.

This paper compares mechanical and thermal unfolding of a model protein, finding incompatible free energy landscapes and challenging interpretations of zero-force quantities.

This study shows how protein folding modulates the adhesion strategy of Gram positive pathogens by switching between reversible and irreversible bonding under different mechanical forces.

This paper introduces a novel magnetic tweezers design to study protein folding under force, revealing that protein L transitions to weak collapsed states before folding into its native conformation.

This study shows disulfide bonds in titin Ig domains amplify mechanical power during muscle contraction by enabling high-force folding, boosting power output from 0 to 6,000 zeptowatts at 6.0 pN.

This paper designs a peptide that blocks isopeptide bond formation in pilin proteins, reducing mechanical stability and demonstrating a potential strategy for anti-adhesive antibiotics.