Institute for Protein Research

Laboratory of Molecular Biophysics

Research Interests

1. Structure of pHtrII membrane proteins, for transmitting light signals, and halorhodopsin, for light-driven ion pumping.
2. Development of high-sensitivity NMR using hyperpolarization by terahertz wave irradiation.
3. Structural analysis using NMR bioinformatics.
4. Protein–protein interactions for clock and signal transduction.

Solid–state NMR reveals the structures and functions of biologically important molecular complexes that are not amenable to X-ray crystallography or to solution NMR. These systems include proteins that are tightly bound to lipid bilayers and noncrystalline large molecular complexes, such as the membrane protein pHtrII, for the transmission of light signals, and halorhodopsin, for light-driven ion pumping, transmembrane domains of the proton ATP synthase, and model G-protein-receptor complexes. We apply advanced NMR experimental techniques to problems in bioinformatics and molecular biology. One of our NMR spectrometers features a high-power terahertz wave source, a gyrotron, for enhancing detection sensitivity using electron spin polarization.