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Significance All proteins are synthesized by the ribosome and therefore have the opportunity to fold for the first time while they are still attached to it. Although protein folding in vitro has been extensively characterized, we are just beginning to understand how proteins fold on the ribosome, which is essential to understanding protein folding in vivo. Here, we characterize and compare the folding pathway of a single protein domain on the ribosome and in bulk solution. By probing the response of the protein to mechanical force, chemical denaturant, and point mutations, and comparing experimental results to simulations, we show that this single protein domain folds through the same pathway on and off the ribosome.

A small single-domain protein folds through the same pathway on and off the ribosome