Laboratories & Administration Office
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- Laboratories & Administration Office
- Division of Protein Structural Biology
Laboratory of Protein Folding
member
| Director | Yuji GOTO |
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| Instructor | Kazumasa SAKURAI Hisashi YAGI |
Correspondence
| Tel | 81-6-6879-8614 |
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| Fax | 81-6-6879-8616 |
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| URL | http://www.protein.osaka-u.ac.jp/physical/index.html |
Research
Protein folding is a process in which an extended polypeptide chain acquires a unique folded conformation with biological activity. Clarifying the mechanism of protein folding is essential to improve our understanding of the structure and function of proteins. It is also important because many critical biological processes and disease states involve protein misfolding and aggregation reactions. We are studying the mechanism of conformational stability and protein folding with various physicochemical approaches including NMR, CD, IR and calorimetry.
<Fig.1>
The AFM image of β2-microglobulin amyloid fibrils.
<Fig.2>
The developed system for the single molecule
observations of protein folding dynamics.
Current Research Programs
1) Early folding dynamics of proteins
2) Folding and conformational property of β-lactoglobulin
3) Structure and formation mechanism of amyloid fibrils
4) Conformation and folding of ferredoxin-NADP+ reductase
References
1. A rapid flow mixer with 11-μs mixing time microfabricated by a pulsed-laser ablation technique: observation of a barrier-limited collapse in cytochrome c folding. Matsumoto, S. et al. (2007) J. Aml.Chem. Soc. 129, 3840-3841.
2. Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity. Konuma, T. et al. (2007) J. Mol. Biol. 368, 209-218.
3. 3D structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR. Iwata, K. et al. (2006) Proc. Natl. Acad. Sci. USA 103, 18119-18124.
4. Flow-induced alignment of amyloid protofilaments revealed by linear dichroism. Adachi, R. et al. (2007) J. Biol. Chem. 282, 8978-8983.
5. Cores and pH-dependent dynamics of ferredoxin-NADP+ reductase revealed by hydrogen/deuterium exchange. Lee, Y. H. et al. (2007) J. Biol. Chem. 282, 5959-5967.
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