Areas of Interest
Proteins start life as linear amino acid sequences and end up as beautifully folded, active structures. Dr. Bardwell's laboratory focuses on recently discovered machinery that drives protein folding in the cell. Powerful genetic, structural, and biophysical tools are being used to generate a detailed picture of how these folding machines work. Members of the Bardwell lab also use directed evolution to improve protein folding. They do this by asking organisms themselves to solve difficult protein-folding problems. By examining the solutions to these problems, they are better able to understand folding in the cell.
Honors & Awards
Elected Fellow, American Association for the Advancement of Science, 2013
Rowena G. Matthews Collegiate Professorship, University of Michigan, 2009
HHMI Investigator, 2005
Published Articles or Reviews
Recent Publications
A glimpse into TriC's magic chamber of secrets.
Bardwell JCA.
Cell. 2022; 185: 4679–81.
Trigger factor both holds and folds its client proteins.
Wu K, Minshull TC, Radford SE, Calabrese AN, Bardwell JCA.
Nat Commun. 2022; 13: 4126.
The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase.
Choudhary V, Wu K, Zhang Z, Dulchavsky M, Barkman T, Bardwell JCA, Stull F.
J Biol Chem. 2022; 298: 102251.
ATP-Independent Chaperones.
Mitra R, Wu K, Lee C, Bardwell JCA.
Annu Rev Biophys. 2022; 51: 409–29.
Polyphosphate drives bacterial heterochromatin formation.
Beaufay F, Amemiya HM, Guan J, Basalla J, Meinen BA, Chen Z, Mitra R, Bardwell JCA, Biteen JS, Vecchiarelli AG, Freddolino PL, Jakob U.
Sci Adv. 2021; 7: eabk0233.
Mechanism of the small ATP-independent chaperone Spy is substrate specific.
Mitra R, Gadkari VV, Meinen BA, van Mierlo CPM, Ruotolo BT, Bardwell JCA.
Nat Commun. 2021; 12: 851.
A cytochrome c is the natural electron acceptor for nicotine oxidoreductase.
Dulchavsky M, Clark CT, Bardwell JCA, Stull F.
Nat Chem Biol. 2021; 17: 344–50.
For a list of publications from PubMed, click HERE