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Showing 1–6 of 6 results
Advanced filters: Author: Philipp Koldewey Clear advanced filters

  • Spy is an ATP-independent chaperone that resides in the Escherichia coli periplasm and promotes the folding of its client Im7. Kinetic analyses now reveal that Im7 folds into its native state while it is bound to Spy.

    • Frederick Stull
    • Philipp Koldewey
    • James C A Bardwell
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 53-58

  • Building crystal structures into the electron density is an important step in protein structure solution. Here, the authors recruit online game players, students, and experienced crystallographers to compete in a competition to solve a new structure, and find that crowdsourcing model-building works.

    • Scott Horowitz
    • Brian Koepnick
    • James C. A. Bardwell
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-11

  • READ is a new crystallographic approach to visualize conformational ensembles of heterogeneous and dynamic molecules. READ is applied here to structurally characterize the various folding states of client Im7 bound to chaperone Spy.

    • Scott Horowitz
    • Loïc Salmon
    • James C A Bardwell
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 691-697

  • Genetic selection uncovers a novel periplasmic chaperone called Spy, whose expression is strongly induced by conditions that cause protein unfolding. Spy can suppress protein aggregation and promote refolding in an ATP-independent manner in vitro. The crystal structure of Spy reveals a thin, cradle-shaped dimer that might shield aggregation-prone regions exposed in unfolded substrates.

    • Shu Quan
    • Philipp Koldewey
    • James C A Bardwell
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 262-269