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Article

Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.

Nature chemistry - 1 Dec 2021

Cassaignau Anaïs M E, Włodarski Tomasz, Chan Sammy H S, Woodburn Lauren F, Bukvin Ivana V, Streit Julian O, Cabrita Lisa D, Waudby Christopher A, Christodoulou John

Abstract excerpt

Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that interactions between the emerging polypeptide and the ribosome surface might allow the ribosome itself to modulate co-translational folding. Here we combine protein engineering and NMR spectroscopy to characterize a series of interactions between the ribosome surface and unfolded nascent chains of the immunoglobulin-like...

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Identifiers

PMID: 34650236
DOI: 10.1038/s41557-021-00796-x
PMCID: PMC8627912

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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