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Showing 1–4 of 4 results
Advanced filters: Author: Stephan Wickles Clear advanced filters

  • Membrane protein topogenesis is not fully understood, although the path that proteins take through the ribosome and Sec-complex has been described. Here, Bischoff et al.present the structure of a ribosome-SecY complex containing an intermediate of proteorhodopsin, which provides further insight into this topogenesis.

    • Lukas Bischoff
    • Stephan Wickles
    • Roland Beckmann
    Research
    Nature Communications
    Volume: 5, P: 1-8

  • Using a family of spectrin domain variants and a combination of structural, biochemical and biophysical approaches, it is shown that cotranslational folding cannot be predicted on the basis of the folding behavior of isolated proteins.

    • Ola B Nilsson
    • Adrian A Nickson
    • Jane Clarke
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 221-225

  • The eukaryotic ribosome-associated complex (RAC) chaperone is poorly understood. Structural analyses now provide insight into the catalytic inactivity and possible functions of the Ssz1 subunit and reveal that RAC interacts with the ribosome via the Zuo1 subunit. RAC crouches over the ribosomal exit tunnel, where its conformation may be controlled by the ribosomal expansion segment ES27.

    • Christoph Leidig
    • Gert Bange
    • Irmgard Sinning
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 23-28