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Showing 1–8 of 8 results
Advanced filters: Author: David Rodriguez-Larrea Clear advanced filters

  • Protein unfolding and translocation through membrane pores occurs in several biological processes and has implications in nanopore technologies. Here, the authors show that the kinetics of unfolding differ depending on which end of the chain enters the pore first.

    • David Rodriguez-Larrea
    • Hagan Bayley
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-7

  • This Perspective describes new single-molecule protein sequencing and identification technologies alongside innovations in mass spectrometry that will eventually enable broad sequence coverage in single-cell proteomics.

    • Javier Antonio Alfaro
    • Peggy Bohländer
    • Chirlmin Joo
    Reviews
    Nature Methods
    Volume: 18, P: 604-617

  • Thioredoxins (Trxs) reduce disulfide bonds via a Michaelis-Menten mechanism. Upon substrate stretching at high forces, an SN2 reaction can be used by bacterial Trxs. A third mechanism, single-electron transfer, is now revealed in Trxs of either bacterial or eukaryotic origin, and is correlated with the depth of the Trx substrate-binding groove.

    • Raul Perez-Jimenez
    • Jingyuan Li
    • Julio M Fernandez
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 890-896

  • Feng et al address the technical challenge of monitoring the protein folding during membrane translocation. Using thioredoxin as a model and with electric potential driving its translocation through single a-hemolysin nanopore, they observe that after translocation, folding is slower than in bulk due to existence of kinetic traps.

    • Jianfei Feng
    • Pablo Martin-Baniandres
    • David Rodriguez-Larrea
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-11

  • Rosen et al showed, at the single-molecule level, that a protein fluctuates between the native and an intermediate state during its forced translocation through a transmembrane pore, and the kinetics of fluctuations provide the free energy landscape as a function of force. They show further that apparently minor events, like the binding of a divalent metal ion, can have major impacts on the translocation kinetics.

    • Christian Bech Rosen
    • Hagan Bayley
    • David Rodriguez-Larrea
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-9