In our lab, we study how proteins/protein assemblies express their functions based on the information of their 3-dimensional (3D) molecular structures. We combine nuclear magnetic resonance (NMR) spectroscopy, molecular biological techniques, and bioinformatics methods to determine protein structures in atomic-resolution.

We also develop methods and instruments for solid-state NMR spectroscopy. Instrumentation for dynamic nuclear polarization (DNP) that enables orders of magnitude sensitivity improvement deserves most of our time and efforts. Methods for non-uniform data sampling (NUS) and for fast MAS-proton detection techniques would also take an important part of the development.

We mainly focus our attention on signal/ion transducing membrane proteins and functional/pathogenic fibrous protein assemblies. Studying behaviors of these systems in intact cells is also one of the main projects. On-going collaboration with the University Hospital is interested in potential relationships between morphology of pathogenic fibrils and disease phenotypes.

To share protein 3D coordinates together with the NMR parameters worldwide, we also maintain databases PDBj as well as BioMagResBank (BMRB).