Amir Bitran @amirbitran.bsky.social · Jul 5 But something wildly different happens for HaloTag, which attains higher folding yield when translated vs refolded from denaturant. Turns out HT hardly folds on the ribosome, showing only weak HDX protection But once released, it folds through a different intermediate than when refolded! (7/n)
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This is really important since the refolding intermediate upon denaturant dilution is known to aggregate. The ribosome thus introduces a “memory” of sorts that biases the protein to avoid this intermediate and the problematic aggregation. (8/n).