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
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.
A metabolite binding protein moonlights as a bile-responsive chaperone.
Lee C, Betschinger P, Wu K, Żyła DS, Glockshuber R, Bardwell JCA.
EMBO J. 2020; 39: e104231.
Yeast tripartite biosensors sensitive to protein stability and aggregation propensity.
Sachsenhauser V, Deng X, Kim HH, Jankovic M, Bardwell JCA.
ACS Chem Biol. 2020; 15: 1078–88.
SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins.
Meinen BA, Gadkari VV, Stull F, Ruotolo BT, Bardwell JCA.
Proc Natl Acad Sci U S A. 2019; 116: 23040–49.
Protein folding while chaperone bound is dependent on weak interactions.
Wu K, Stull F, Lee C, Bardwell JCA.
Nat Commun. 2019; 10: 4833.
For a list of publications from PubMed, click HERE