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Updated: Aug 17, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
Published on: February 12, 2019
Cotranslational folding of human growth hormone in vitro and in Escherichia coli
Daphne Mermans1, Felix Nicolaus1, Aysel Baygin1
1Department of Biochemistry and Biophysics, Stockholm University, Sweden.
Abstract:
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.
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