This is a decommissioned version of ERA which is running to enable completion of migration processes. All new collections and items and all edits to existing items should go to our new ERA instance at https://ualberta.scholaris.ca - Please contact us at erahelp@ualberta.ca for assistance!
- 72 views
- 294 downloads
Single-Molecule Force Spectroscopy of Protein Folding
-
- Author(s) / Creator(s)
-
The use of force probes to induce unfolding and refolding of single molecules through the application of mechanical tension, known as single-molecule force spectroscopy (SMFS), has proven to be a powerful tool for studying the dynamics of protein folding. Here we provide an overview of what has been learned about protein folding using SMFS, from small, single-domain proteins to large, multi-domain proteins. We highlight the ability of SMFS to measure the energy landscapes underlying folding, to map complex pathways for native and non-native folding, to probe the mechanisms of chaperones that assist with native folding, to elucidate the effects of the ribosome on co-translational folding, and to monitor the folding of membrane proteins.
-
- Date created
- 2021-10-01
-
- Type of Item
- Article (Draft / Submitted)