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
2013 Fellow, American Association for the Advancement of Science
2009 Rowena G. Matthews Collegiate Professorship, University of Michigan
2005 HHMI Investigator
Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.
Yan Z, Hussain S, Xu W, Bernstein HD, Bardwell JCA.
Mol Microbiol. 2019, in press.
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.
Periplasmic Chaperones and Prolyl Isomerases.
Stull F, Betton JM, Bardwell JCA.
EcoSal Plus. 2018. doi: 10.1128/ecosalplus.ESP-0005-2018.
Electrostatic interactions are important for chaperone-client interaction in vivo.
Lee C, Kim H, Bardwell JCA.
Microbiology. 2018; 164: 992-7.
Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ).
Salmon L, Ahlstrom LS, Bardwell JCA, Horowitz S.
Methods Mol Biol. 2018; 1764: 491-504.
Folding against the wind.
Stull F, Bardwell JCA.
Nat Chem Biol. 2018; 14: 329-30.
For a list of publications from PubMed, click HERE