Snapshots of co-translational multi-domain protein folding

Abstract

Understanding how proteins fold is of extreme importance in biology. Increasing evidence show that protein folding is commonly initiated during synthesis while the nascent polypeptide is still bound to the ribosome. However, there is limited information on how this large macromolecule complex is involved in the whole process. Therefore, we aim to extend our understanding of co-translational folding. We make use of single molecule FRET (smFRET) to determine conformational changes on the protein by analyzing snapshots of the nascent chain at different lengths during synthesis.