SEISAN KENKYU
Online ISSN : 1881-2058
Print ISSN : 0037-105X
ISSN-L : 0037-105X
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Displaying 1-6 of 6 articles from this issue
Introduction to Special Section
Research Review
  • Shizuka NAKANO, Rieko MURAMATSU, Yukiko T. MATSUNAGA
    Article type: Research Review
    2022 Volume 74 Issue 2 Pages 147-151
    Published: May 01, 2022
    Released on J-STAGE: May 27, 2022
    JOURNAL FREE ACCESS

    Cellular communication is important to regulate the disease progression in the central nervous system (CNS). Microfluidics device, which is characterized by well-controlled culture environments, is a useful system to evaluate cellcell interactions under the pathological condition of the CNS. Here, we introduce the recent advances of the microfluidics devices which enable to evaluate the CNS pathology.

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  • Ryota NAKAOKA, Toshiyuki HIRANO, Fumitoshi SATO
    Article type: Research Review
    2022 Volume 74 Issue 2 Pages 153-159
    Published: May 01, 2022
    Released on J-STAGE: May 27, 2022
    JOURNAL FREE ACCESS

    Interferon (IFN) α2 is a 165-residue protein, and there is a recombinant IFN α2b that differs from the wild strain (IFN α2a) only at the 23rd residue of the amino acid sequence (Lys23Arg). IFN α2a can bind to the interferon receptor (IFNAR2). The 23rd amino acid is not in direct contact with IFNAR2, but IFN α2b is known to be more active than IFN α2a. In this study, in order to investigate the cause of difference, we performed canonical molecular orbital calculations and examined the difference in electronic states associated with the mutation. The results of electrostatic potential and Milliken charges suggest that the difference of Lys23Arg may produce a gain in the Coulomb force.

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  • Tianyu WANG, Toshiyuki HIRANO, Fumitoshi SATO
    Article type: Research Review
    2022 Volume 74 Issue 2 Pages 161-167
    Published: May 01, 2022
    Released on J-STAGE: May 27, 2022
    JOURNAL FREE ACCESS

    PETase is an enzyme that can decompose polyethylene terephthalate (PET). The explanation behind PETase’s ability to decompose PET remains still unknown. In this study, canonical molecular orbital (CMO) calculation of the active site of PETase was carried out. The results indicated that the electronic structure of PETase’s catalytic triad was preserved, and the nucleophilic property of Serine’s hydroxyl oxygen was proved, implying that amino acid residues surrounding the catalytic triad may protect the catalytic triad’s electronic structure.

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