|Associate Professor||Yoh MATSUKI|
|Assistant Professor||Ayako EGAWA
|Technical Staff||Naoyuki ABE|
We are studying the structure and function of the biological macromolecular systems mainly by using nuclear magnetic resonance (NMR). NMR provides information on the protein structure and dynamics at work with atomic resolution. Taking this advantage, we can understand biological activities for energy conversion and signal transduction systems. Since proteins play key roles through the intermolecular interactions in complex systems such as cells and supramolecules, we are also developing state-of-art solution and solid-state NMR methodologies including isotope-labeled sample preparation techniques and NMR bioinformatics. One of our programs for high-resolution solid-state NMR features high-field dynamic nuclear polarization (DNP) at cryogenic temperatures for a 10000-fold signal enhancement by using high-intensity terahertz light source, gyrotron.
Current Research Programs
- Structure, interaction and function of protein systems as revealed by NMR
- Solution and solid-state NMR for cellular and supramolecular systems
- Development of high-resolution NMR using hyper-polarized spins
- Utilization of lysine 13C-methylation NMR for protein-protein interaction studies. Hattori Y, Furuita K, Ohki I, Ikegami T, Fukada H, Shirakawa M, Fujiwara T, Kojima C (2013) J. Biomol. NMR 55, 19-31.
- Secondary Structural Analysis of proteins based on 13C chemical shift assignments in unresolved solid-state NMR spectra enhanced by fragmented structure database, Ikeda K, Egawa A, Fujiwara T (2013) J. Biomol. NMR 55, 189-200.
- Helium-cooling and -spinning dynamic nuclear polarization for sensitivity-enhanced solid-state NMR at 14 T and 30 K, Matsuki Y, Ueda K, Idehara T, Ikeda R, Ogawa I, Nakamura S, Toda M, Anai T, Fujiwara T (2012) J. Magn. Reson. 225, 1-9.
- 14-3-3 proteins act as intracellular receptors for rice Hd3a florigen, Taoka K, Ohki I, Tsuji H, Furuita K, Hayashi K, Yanase T, Yamaguchi M, Nakashima C, Purwestri YA, Tamaki S, Ogaki Y, Shimada C, Nakagawa A, Kojima C, Shimamoto K (2011) Nature 476, 332-335.