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. James Bardwell’s lab also uses 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.
Dr. Bardwell received his Ph.D. from the University of Wisconsin at Madison in 1987 and was a post doctoral fellow at Harvard Medical School. He has been a Fellow of the Alexander von Humboldt Foundation and held a Visiting Professor appointment in Regensburg, Germany.
Ricky Stull, Postdoctoral Fellow
Changhan Lee, Postdoctoral Fellow
Zhen Yan, Postdoctoral Fellow
Honors & Awards
2013 AAAS Fellow, American Association for the Advancement of Science
2009 Rowena G. Matthews Collegiate Professorship
2005-Present HHMI Investigator
Selected Published Articles or Reviews
Horowitz S, Koldewey P, Stull F, Bardwell JC. Folding while bound to chaperones. Curr Opin Struct Biol. 2017 Jul 19;48:1-5. doi: 10.1016/j.sbi.2017.06.009. [Epub ahead of print] Pubmed
Koldewey P, Horowitz S, Bardwell JCA. Chaperone-client interactions: Non-specificity engenders multifunctionality. J Biol Chem. 2017 Jul 21;292(29):12010-12017.
Horowitz S, Koepnick B, Martin R, Tymieniecki A, Winburn AA, Cooper S, Flatten J, Rogawski DS, Koropatkin NM, Hailu TT, Jain N, Koldewey P, Ahlstrom LS, Chapman MR, Sikkema AP, Skiba MA, Maloney FP, Beinlich FR; Foldit Players; University of Michigan students, Popović Z, Baker D, Khatib F, Bardwell JC. (2016). Determining crystal structures through crowdsourcing and coursework. Nat. Commun.2016 Sep 16;7:12549. doi: 10.1038/ncomms12549. Pubmed
Koldewey P, Stull F, Horowitz S, Martin R, Bardwell JCA. (2016) Forces Driving Chaperone Action. Cell. 2016 Jul 14;166(2):369-379
Horowitz S, Salmon L, Koldewey P, Ahlstrom L, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JCA. (2016) Visualizing Chaperone-assisted Folding. Nature Struct. Mol. Biol. 2016 Jul;23(7):691-7.
Stull F, Koldewey P, Humes JR, Radford SE, Bardwell JC. (2016). Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nat Struct Mol Biol. 2016 Jan;23(1):53-8.
Lennon CW, Thamsen M, Friman ET, Cacciaglia A, Sachsenhauser V, Sorgenfrei FA, Wasik MA, Bardwell JC. (2015) Folding Optimization In Vivo Uncovers New Chaperones. J Mol Biol. Sep 11;427(18):2983-94
Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC. (2014) Super Spy variants implicate flexibility in chaperone action. Elife. 2014;3:e01584.
Foit L, George JS, Zhang BW, Brooks CL 3rd, Bardwell JC. (2013) Chaperone activation by unfolding. Proc Natl Acad Sci U S A. 110(14):E1254-62.
Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. (2011) Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol. 18(3):262-9.
Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. (2010) Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A. 107(3):1071-6.
Foit L, Morgan GJ, Kern MJ, Steimer LR, von Hacht AA, Titchmarsh J, Warriner SL, Radford SE, Bardwell JC.. (2009)Optimizing protein stability in vivo. Mol Cell. Dec 11;36(5):861-71.
For a list of publications from PubMed, click HERE