Svend Kjær

Jul 10, 2024 | nature.com | Thomas E. Wales |Svend Kjær |F. Ulrich Hartl |John Engen

AbstractProtein folding in vivo begins during synthesis on the ribosome and is modulated by molecular chaperones that engage the nascent polypeptide. How these features of protein biogenesis influence the maturation pathway of nascent proteins is incompletely understood. Here, we use hydrogen–deuterium exchange mass spectrometry to define, at peptide resolution, the cotranslational chaperone-assisted folding pathway of Escherichia coli dihydrofolate reductase.