The ribosome stabilizes partially folded intermediates of a nascent multi-domain protein.

ABSTRACT: Co-translational folding is crucial to ensure the production of biologically active proteins. The ribosome can alter the folding pathways of nascent polypeptide chains, yet a structural understanding remains largely inaccessible experimentally. We have developed site-specific labelling of nascent chains to detect and measure, using ¹⁹F nuclear magnetic resonance (NMR) spectroscopy, multiple states accessed by an immunoglobulin-like domain within a tandem repeat protein during biosynthesis. By examining ribosomes arrested at different stages during translation of this common structural motif, we observe highly broadened NMR resonances attributable to two previously unidentified intermediates, which are stably populated across a wide folding transition. Using molecular dynamics si

SUBMITTER: Chan SHS 

PROVIDER: S-EPMC7613651 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature