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- W4211107671 abstract "All proteins are synthesized by the ribosome and the relatively slow nature of this process allows for nascent proteins to sample conformational space before synthesis is complete. This search differs significantly from re-folding: translation is vectorial and the folding environment near the ribosome is highly charged and sterically restricted. While much is known about in vitro refolding, to date, our understanding of the co-translational process has been hampered by the lack of tools to monitor biophysical properties in the complex non-equilibrium environment required for co-translational folding." @default.
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- W4211107671 date "2022-02-01" @default.
- W4211107671 modified "2023-09-28" @default.
- W4211107671 title "Monitoring protein folding on and off the ribosome using structural mass spectrometry approaches" @default.
- W4211107671 doi "https://doi.org/10.1016/j.bpj.2021.11.1797" @default.
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