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- W2790068744 abstract "We have developed a strategy to enable the study of co-translational folding using solution-state NMR spectroscopy, the only technique able to characterize this dynamic process at atomic resolution. Using isotopically-labelled, ribosome-nascent chain complexes (RNCs), we have created snapshots that mimic the emergence of an immunoglobulin-like domain, FLN5, within a multidomain protein. The ribosome appears to modulate the folding process, as the complete sequence of FLN5 is required to emerge well beyond the tunnel before acquiring native structure, whereas FLN5 in isolation folds spontaneously, even when truncated. To understand the behaviour of this nascent chain while bound to the ribosome, we use a combination of protein engineering and NMR dynamics to describe residue-specific sites of nascent-chain-ribosome interactions of different magnitude of strength, and biochemical assays as well as chemical shift-restrained MD simulations of RNCs to underpin our spectral observations. The multi-pronged studies presented here are providing some of the first high-resolution insights of these fundamental processes, and begin to dissect the energy landscape sampled by a nascent chain on the cusp of initiation of folding on the ribosome. 1. Cassaignau, Cabrita et al., NSMB 2016 2. Cassaignau et al., Nat Prot 2016" @default.
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- W2790068744 date "2018-02-01" @default.
- W2790068744 modified "2023-10-17" @default.
- W2790068744 title "Structures and Dynamics of Protein Folding on the Ribosome by NMR Spectroscopy" @default.
- W2790068744 doi "https://doi.org/10.1016/j.bpj.2017.11.2294" @default.
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