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Clarification of hierarchical dynamics in protein

Nakagawa, Hiroshi   ; Inoue, Rintaro*; Oda, Takashi*; Yagi-Utsumi, Maho*; Saio, Tomohide*; Oroguchi, Tomotaka*; Nagata, Yuya*; Sugiyama, Masaaki*; Sato, Mamoru*; Kawakita, Yukinobu  ; Iwase, Hiroki*; Tominaga, Taiki*; Takata, Shinichi  

Proteins have hierarchical structures and hierarchical dynamics. Neutron scattering is expected to be a promising experimental technique to study the hierarchical structure on the nanometer order related to biological functions and the structure and dynamics on the pico- to nanosecond time scale. The research was initiated with the aim of elucidating the structure and dynamics of these spatiotemporal scales (MLF Long-term Proposal 2019L0300). In this proposal, we used samples of characterized functional multidomain proteins, including folded proteins and naturally denatured proteins, to promote our research. Researchers in a wide range of specialized fields collaborated to develop "a protein partial deuteration method utilizing the features of neutron scattering", "a wide spatio-temporal seamless analysis method by linking various neutron spectrometers", "a method for visualizing protein dynamics by linking neutron and computational science," and "a neutron quasi-elastic scattering measurement method for dilute protein solutions" and to We have pioneered a new generation of neutron structural biology that will lead protein science in Japan.



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