Cotranslational folding of human growth hormone in vitro and in Escherichia coli

Human growth hormone (hGH) is a four‐helix bundle protein of considerable pharmacological interest. Recombinant hGH is produced in bacteria, yet little is known about its folding during expression in Escherichia coli. We have studied the cotranslational folding of hGH using force profile analysis (FPA), both during in vitro translation in the absence and presence of the chaperone trigger factor (TF), and when expressed in E. coli. We find that the main folding transition starts before hGH is completely released from the ribosome, and that it can interact with TF and possibly other chaperones. Human growth hormone (hGH) is a four‐helix bundle protein of considerable pharmacological interest. Recombinant hGH is produced in bacteria, yet little is known about its folding during expression in Escherichia coli. We show that hGH starts to fold before it is completely released from the ribosome, and that it can interact with chaperones during folding.