Despite much progress over the last six decades, we are still far from understanding the mechanism of protein folding and aggregation in the cell. This lack of information poses tremendous challenges to progress in many areas of life sciences and biomedical research. In bacteria, the majority of soluble cellular proteins fold or aggregate co-translationally and immediately post-translationally. The ribosome plays a key role in this process. This presentation will report progress on our molecular-level understanding of how the ribosome, ribosomal proteins and cotranslationally active molecular chaperones modulate the balance between protein folding and aggregation in the cell. By probing the structure and dynamics of nascent proteins by fluorescence lifetime and depolarization, single-particle cryo-electron microscopy, multidimensional NMR, biochemical tools and kinetic simulations, we will attempt to highlight some fundamental concepts of general significance. Finally, we will show how further insights can be achieved upon exploiting novel optically enhanced nuclear magnetic resonance technologies in solution.

The early stages of protein folding and aggregation in the cell: adventures in light-, electron- and magnet-assisted chemical biology

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.