Abstract:Multi‐domain proteins – constituting a large group in all proteomes – often require help from molecular chaperones to fold productively, even before the ribosome has finished their synthesis. The mechanisms underlying chaperone function remain poorly understood. We have used optical tweezers to study the folding of elongation factor G (EF‐G), a model multi‐domain protein, as it emerges from the ribosome. We find that the N‐terminal G‐domain in nascent EF‐G polypeptides folds robustly. The following domain II, … Show more
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