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Showing 1–16 of 16 results
Advanced filters: Author: Georg Krainer Clear advanced filters

  • pH is a critical regulator of (bio)chemical processes and therefore tightly regulated in nature. Now, proteins have been shown to possess the functionality to drive pH gradients without requiring energy input or membrane enclosure but through condensation. Protein condensates can drive unique pH gradients that modulate biochemical activity in both living and artificial systems.

    • Hannes Ausserwöger
    • Rob Scrutton
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Chemistry
    P: 1-12

  • Biomolecular phase separation arises from collective molecular interactions and is emerging as a key theme for biological function. Here the authors propose a broadly applicable method to quantify these interactions based on compositional and energetic parameters.

    • Hannes Ausserwöger
    • Ella de Csilléry
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • Physical characterisation of proteins is challenging. Here the authors report single-molecule microfluidic diffusional sizing (smMDS) to enable calibration-free single-molecule diffusional-sizing based monitoring of protein hydrodynamic radii even within heterogenous multicomponent mixtures.

    • Georg Krainer
    • Raphael P. B. Jacquat
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-19

  • The formation of protein aggregates is a hallmark of Parkinson’s disease, with small oligomeric species implicated as a major source of toxicity. In this work, Xu et al. determine their mechanism of formation and role in aggregation.

    • Catherine K. Xu
    • Georg Meisl
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-11

  • Georg Krainer and Antoine Treff et al. use a helical-hairpin construct derived from the cystic fibrosis transmembrane conductance regulator (CFTR) to investigate misfolding caused by the disease-linked V232D mutation. Using single-molecule FRET, they show that the V232D hairpin assumes an open conformation in lipid bilayers, which is reversed by the pharmacological corrector Lumacaftor.

    • Georg Krainer
    • Antoine Treff
    • Michael Schlierf
    ResearchOpen Access
    Communications Biology
    Volume: 1, P: 1-7

  • There are limitations with current protein sensing methods. Here the authors report DigitISA, a digital immunosensor assay based on microchip electrophoretic separation and single-molecule detection that enables quantitation of protein biomarkers in a single, solution-phase step.

    • Georg Krainer
    • Kadi L. Saar
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-21

  • A central concept for characterising phase-separating systems is the phase diagram but generation of such diagrams for biomolecular systems is typically slow and low-throughput. Here the authors describe PhaseScan, a combinatorial droplet microfluidic platform for high-resolution acquisition of multidimensional biomolecular phase diagrams.

    • William E. Arter
    • Runzhang Qi
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • Molecular chaperones from the Hsp70 family can break up protein aggregates, including amyloids. Here, the authors utilize microfluidic diffusional sizing to assess the mechanism of α-synuclein (αS) disaggregation by the Hsc70–DnaJB1–Apg2 system, and show that single αS molecules are removed directly from the fibril ends.

    • Matthias M. Schneider
    • Saurabh Gautam
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11

  • Elucidating the molecular driving forces underlying liquid–liquid phase separation is a key objective for understanding biological function and malfunction. Here the authors show that a wide range of cellular proteins, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, which form condensates at low salt concentrations, can reenter a phase-separated regime at high salt concentrations.

    • Georg Krainer
    • Timothy J. Welsh
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • In this work the authors describe antimicrobial peptides (AMPs)-driven phase transitions of intracellular nucleic acids, whereby AMPs induce compaction and phase separation of nucleic acids, resulting in their sequestration and eventual cell death.

    • Tomas Sneideris
    • Nadia A. Erkamp
    • Tuomas P. J. Knowles
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-16