Science at the Edge Seminar
- Sep 29, 2017
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Speaker: James Bardwell, Molecular, Cellular & Developmental Biology, University of Michigan
Title: Watching a Chaperone Fold a Protein at High Resolution
Refreshments at 11:15 am.
Date: Fri, 29 Sep 2017, 11:30 am – 12:30 pm
Location: 1400 BPS Bldg.
The Bardwell laboratory has addressed four of the central mysteries of chaperone biology: how chaperones rapidly bind to proteins, how the chaperone-substrate complex is stabilized, how a chaperone can facilitate substrate folding, and what triggers substrate release1,2. The laboratory has also devised a novel structural biology approach that enabled us to visualize the dance of chaperone-mediated folding1,4 demonstrating that client folding occurs while bound to the chaperone3.
- Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Pavel V, Afonine PV, Bedem H, Wang L, Xu Q, Trievel RC, Brooks III CL, and Bardwell JCA (2016) Visualizing chaperone-assisted folding Nature Struct. Mol. Biol. 23:691-7 PMID: 27239796
- Philipp Koldewey, Frederick Stull, Scott Horowitz, Raoul Martin, and James C. A. Bardwell (2016) Forces Driving Chaperone Action Cell 166(2):369-79 PMID: 27293188
- Stull F, Koldewey P, Humes JR, Radford SE, and Bardwell JCA (2016) Substrate protein folds while it is bound to the ATP-independent chaperone Spy Nature Struct. Mol. Biol. 23:53-8. PMID: 2661926
- Salmon L, Ahlstrom LS, Horowitz S, Dickson A, Brooks CL 3rd, Bardwell JC. (2016) Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling. J Am Chem Soc. 138(31):9826-39. PMID:27415450
Bardwell publications can be found by following this link:
Dr. Bardwell was a graduate student at the University of Wisconsin with Elizabeth Craig. He was a postdoctoral researcher with John Beckwith at Harvard University. He was a Visiting Professor and Alexander von Humboldt Fellow at the Institute of Biophysics and Physical Biochemistry, University of Regensburg, Germany, before joining the faculty at the University of Michigan.