奈良先端科学技術大学院大学 物質創成科学領域

Education and Research Activities in the Laboratory

The concerted actions of various molecules result in high-order functions that cannot be realized by individual molecules, as seen in various biological systems. The Complex Molecular Systems Laboratory, established on April 1, 2015, currently focuses on the complex molecular systems involving multicomponent biological molecules such as proteins. Weakly and/or strongly coupled proteins undergo regulatory dissociation and association in response to external stimuli, thereby exhibiting advanced biological functions. To determine the physicochemical properties of these molecular systems and to create new functional molecular systems, our laboratory employs various biophysical techniques, such as structural analysis using multiple probes (X-ray, neutron, and electron), spectroscopic measurements, protein engineering, and theoretical analysis. Multidisciplinary knowledge is essential to clearly understand the characteristics of these complex molecular systems. We welcome students with various educational backgrounds such as physics, chemistry, material science, and biology. By enabling students to work on their own research theme independently, we encourage them to develop their own interests and to learn essential research skills, such as identifying problems to be solved, designing experiments that will yield solutions, and comprehensively interpreting experimental results.

Research Themes

1. Development of analytical methods to investigate complex molecular systems (Fig. 1)
2. Investigation of the dynamical ordering of multi-component proteins (Fig. 2)
3. Creation of high-order self-assembled complex molecular systems (Fig. 2)
4. Detailed analysis of intramolecular actions in individual proteins responsible for the dynamical ordering of complex molecular systems in higher-class structural hierarchy (Fig. 3)
5. Development of rational molecular designs for novel synthetic proteins

Recent Research Papers and Achievements

1. K. Yonezawa, N. Shimizu, K. Kurihara, Y. Yamazaki, H. Kamikubo, M. Kataoka. “Neutron crystallography of photoactive yellow protein reveals unusual protonation state of Arg52 in the crystal.” Sci Rep 7(1):9361. (2017).
2. H. Kuramochi, S. Takeuchi, K. Yonezawa, H. Kamikubo, M. Kataoka, T. Tahara, “Probing the early stages of photoreception in photoactive yellow protein with ultrafast time-domain Raman spectroscopy”, Nature Chemistry, 10.1038/nchem.2717 (2017).
3. Y. Yoshimura, N. A. Oktaviani, K. Yonezawa, H. Kamikubo, F. A. A. Mulder, “Unambiguous Determination of the Ionization State of a Photoactive Protein Active Site Arginine in Solution by NMR Spectroscopy”, Angewandte Chemie 56, 239-242 (2017).
4. F. Schotte, H. S. Cho, V. R. I. Kaila, H. Kamikubo, N. Dashdorj, E. R. Henry, T. J. Graber, R. Henning, M. Wulff, G. Hummer, M. Kataoka, P. A. Anfinrud, “Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallography”, Proc. Natl. Acad. Sci. USA 109 19256-19261 (2012).
5. S. Yamaguchi, H. Kamikubo, K. Kurihara, R. Kuroki, N. Niimura, N. Shimizu Y. Yamazaki, M. Kataoka, “Low-barrier hydrogen bond in photoactive yellow protein”, Proc. Natl. Acad. Sci. USA 106 440-444 (2009).