Neutron Scattering (KURRI, Kumatori)

Staff Professor Yukio Morimoto Assistant Professor Akio Kawaguchi
Professor Masaaki Sugiyama Assistant Professor Akiko Kita
Associate Professor Rintaro Inoue Assistant Professor Ken Morishima
Assistant Professor Aya Okuda

Prof. Morimoto: Neutron Scattering Science

Neutron scattering and diffraction is the most powerful technique to investigate and clarify the structure and function of materials, and its effect is more accelerated by collaboration with other methods, such as scattering and diffraction with X-ray or spectroscopic methods. So we have concentrated on neutron scattering studies of structural biology of the macromolecule from viewpoints of hydrogen atoms and bonds, strategic structural research for protein complexes under the crystal and/or solutions, the structure of various kinds of polymeric materials. Also we have actively collaborated with other high-flux facilities: KENS, Tsukuba and J-PARK, JRR-3M, Tokai, and synchrotron radiation sources.

Prof. Sugiyama: Radiation Material Science

It is well known that a material structure and its dynamical character are deeply related. The interaction between the constituents determines the material structure and the dynamical character is a response of the structural interaction against the external disturbances. In the case of a functional material with a nano-scale structure, it is essential to reveal a mechanism of function to understand its dynamical character based on the structure. Along this line, this research group studies the static and dynamical structures of functional materials with nano-scale structures such as supercritical fluid, polymer aggregates, gel and protein. Main methods to measure nano-scale structure are scattering techniques with X-ray or neutron: especially, neutron scattering utilizing its ability identifying isotopes, proton and deuteron, is a very powerful tool to reveal a quaternary structure of protein. Recently, we revealed a state of PA28 (Proteasome Activator 28) in an aqueous solution: PA28 is a regulator protein of the 20S proteasome, which is protease for an ubiquitinated protein. Figure 1 shows the SANS analysis of the state of PA28 in an aqueous solution. The structural simulation well reproduces the experimental SANS profiles. In addition, we are developing a spectrometer and analyzing methods. Therefore, we are joining the TAIKAN project (SANS in J-PARC) and also developing a SANS and SAXS simulation with RMC algorism.

Figure 1: Structural model, SANS profiles. Circles denote experimental data and lines show the result of the simulation.