Institute of Multidisciplinary Research for Advanced Materials, Tohoku University


LAST UPDATE 2021/05/01

  • 研究者氏名
    Researcher Name

    南後恵理子 Eriko NANGO
    教授 Professor
  • 所属
    Professional Affiliation

    Institute of Multidisciplinary Research for Advanced Materials, Tohoku University

    有機・生命科学研究部門 量子ビーム構造生物化学研究分野
    Division of Organic- and Bio-materials Research, Quantum Beam-based Structural Biology and Chemistry
  • 研究キーワード
    Research Keywords

    X-ray free electron lasers
    Time-resolved measurement
Research Subject
Analysis of protein structural dynamics and its application to molecular control

研究の背景 Background


A protein is one of the biomolecules that are essential to the phenomena of life, such as cell signaling, in vivo catalytic reactions, storage and transport. A three-dimensional structure of a protein is closely related to its function. While many protein structures over 160,000 have been determined, most of them are “static structures” under cryogenic temperature. Therefore, it is desired that the dynamic process in which proteins function is elucidated at the atomic level.

研究の目標 Outcome


We are developing techniques using a quantum beam such as an X-ray free-electron laser or synchrotron radiation to visualize actual chemical reaction and structural changes in proteins. We will reveal the reaction mechanism of light-sensitive proteins and the reaction mechanism of enzymes catalyzing unique reactions. Furthermore, we aim to design and create protein molecules with new functions based on precise information from dynamic structural analysis.

研究図Research Figure

Fig.1. Experimental setup for pump–probe time–resolved serial femtosecond crystallography (TR–SFX). An enlarged view around the sample is shown in (b).Fig.2. Pathway for proton transfer in bacteriorhodopsin (bR). View of the |Fobs|light – |Fobs|dark difference map from TR–SFX bR data for Δt = 760 ns. A positive difference feature (arrow) suggests the ordering of a water molecule.Fig.3. Superimposition of bR structural models collected in TR–SFX experiments upon the resting bR structure (purple) for Δt =16 ns (blue),760 ns (red), 36.2 ms (orange), and 1.725 ms (yellow).

文献 / Publications

Struct. Dyn. 7, 024701 (2020). J. Appl. Cryst. 52, 1280 (2019). Science 261, 145 (2018). Nat Commun. 8, 1585 (2017). J. Synchrotron Radiat. 24, 1086 (2017).Nature 543, 131 (2017). Science 354, 1552 (2016).