F. Ulrich Hartl

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.

Jun 19, 2023 | cell.com | Martin Muller |F. Ulrich Hartl

Cookie Preference CenterWe use cookies which are necessary to make our site work. We may also use additional cookies to analyse, improve and personalise our content and your digital experience. For more information, see our Cookie Policy and the list of Google Ad-Tech Vendors. You may choose not to allow some types of cookies. However, blocking some types may impact your experience of our site and the services we are able to offer.