| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 20614 | Journal of Bioscience and Bioengineering | 2013 | 5 Pages |
Abstract
GroEL–protein interactions were characterized by stable isotope-assisted nuclear magnetic resonance (NMR) spectroscopy using chemically denatured bovine rhodanese and an intrinsically disordered protein, α-synuclein, as model ligands. NMR data indicated that proteins tethered to GroEL remain largely unfolded and highly mobile, enabling identification of the interaction hot spots displayed on intrinsically disordered proteins.
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Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Noritaka Nishida, Maho Yagi-Utsumi, Fumihiro Motojima, Masasuke Yoshida, Ichio Shimada, Koichi Kato,