that lead to the desired folded state. Chaperones begin to assist in protein folding as soon as a nascent chain longer than 60 amino acids emerges from the ribosome exit channel.

One of the most studied ribosome binding chaperones is trigger factor (TF). TF works to stabilize the peptide, promotes its folding, prevents aggregation, and promotes refolding of denatured model substrates. Ribosome profiling experiments have shown that TF predominantly targets ribosomes translating outer membrane proteins