Physical Chemistry of Biomolecules Laboratory
The native stereo-regular structure of a protein is determined by the specific amino acid sequence (= genetic information) of the protein. Such a characteristic of the proteins that take major roles in various biological processes, originated in the four billion-year history of biological evolution. Nevertheless, the formation of the stereo-regular structure, i.e., the folding of a protein is a physicochemical process as well, and based on the thermodynamic principle. Elucidation of the molecular mechanism of protein folding is thus a fundamental problem in biophysical chemistry, i.e., the problem that mediates between life and physical matters. Based on this standpoint, we are studying (1) in vitro refolding of model proteins, and (2) action mechanisms of molecular chaperones that mediate the protein folding in biological cells. To this end, we are using various spectroscopic techniques including NMR, physical techniques such as calorimetric measurements, and molecular biological techniques including gene manipulation experiments.
The transition-state structure of folding of a-lactalbumin. Comparison between experimental (A) and simulation (B) results (J. Mol. Biol. 371, 1354-1364 (2007)).
- T. Inobe, K. Takahashi, K. Maki, S. Enoki, K. Kamagata, A. Kadooka, M. Arai & K. Kuwajima: "Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle X-ray scattering," Biophys. J. 94, 1392-1402 (2008)
- T. Oroguchi, M. Ikeguchi, M. Ota, K. Kuwajima & A. Kidera: "Unfolding pathways of goat a-lactalbumin as revealed in multiple alignment of molecular dynamics trajectories," J. Mol. Biol. 371, 1354-1364 (2007)