Professor, Biological Chemistry
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. Two types of folding helpers are being studied, the catalysts responsible for disulfide bond formation and the heat shock proteins, which chaperone protein folding. Powerful genetic, structural, and biophysical tools are being used to generate a detailed picture of how these folding machines work.
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.
1999 Literature, Science and Arts Excellence in Research Award
1997-2001 Pew Scholar
1993-1995 Alexander von Humboldt Fellowship
1989-1993 Helen Hay Whitney Fellowship, NSERC Postgraduate Scholarship
Collet J-F. and Bardwell J.C.A. (2003) Oxidative folding in Bacteria NATO Science series
Collet, J-F. and Bardwell J.C.A. (2005) The Catalysis of disulfide bond formation in Prokaryotes. in Protein Folding Handbook, Buchner/Kiefhaber Eds. Wiley-VCH.
Nakamoto, H. and Bardwell J.C.A. (2004) Catalysis of Disulfide Bond Formation and Isomerization in the Bacterial Periplasm Biochim Biophys Acta 1694:111-9
Hiniker, A. and Bardwell J. C.A. (2004) Disulfide relays between and within proteins: the Erolp structure. Trends in Biochem Sci. 29:516-9
Tan, J. Lu Y, and Bardwell J.C.A. (2005) Mutational Anlysis of the disulfide catalysts DsbA and DsbB. J.Bacteriol. 187: 1504-10.
Bardwell J.C.A. (2005) The dance of disulfide formation. Nat Struct. Mol Biol 11:582-3. PMID: 15221018
Bardwell J.C.A. (2005) Thiol modifications in a snapshot. Nat Biotechnol 23:42-3.
Gleiter, S., and Bardwell, J.C.A. Disulfide bond formation in prokaryotes. Micro. Mol. Biol. Rev. (invited review)
Pan, J., and Bardwell, J.C.A. Thioredoxin-related proteins in E. coli. Protein Science.
Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, and Eisenberg D. (2004) Gram-positive DsbE proteins function differently from gram-negative DsbE homologs: A structure function analysis of DsbE from Mycobacterium tuberculosis. J. Biol. Chem. 279: 3516-24.
Tan, J. and Bardwell, J.C.A. (2004). "Key Players Involved in Disulfide Bond Formation in Prokaryotes." ChemBioChem (in press).
Masip L., Pan J.L., Haldar S., Penner-Hahn J., Georgiou G., Bardwell J.C., and Collet Jean-Francois. (2004). "A de novo engineered pathway for the formation of protein disulfide bonds." Science 303(5661):1185-9.
Kadokura H., Tian H., Zander T., Bardwell J.C., and Beckwith J. (2004). "Snapshots of DsbA in Action: detection of proteins in the process of oxidative folding." Science 303(5657):534-537. PMID: 14739460
Hiniker A. and Bardwell J.C. (2004). "In vivo substrate specificity of periplasmic disulfide oxidoreductases." J. Biol. Chem. [Epub ahead of print]. (Pubmed) PMID: 14726535