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
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.
Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.
Yan Z, Hussain S, Xu W, Bernstein HD, Bardwell JCA.
Mol Microbiol. 2019; 112: 1373-87.
In vivo chloride concentrations surge to proteotoxic levels during acid stress.
Stull F, Hipp H, Stockbridge RB, Bardwell JCA.
Nat Chem Biol. 2018; 14: 1051-8.
Elaborating a coiled-coil-assembled octahedral protein cage with additional protein domains.
Cristie-David AS, Koldewey P, Meinen BA, Bardwell JCA, Marsh ENG.
Protein Sci. 2018; 27: 1893-1900.
For a list of publications from PubMed, click HERE