| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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| Outline of Final Research Achievements |
Ubiquitin phosphorylated at Ser65 (pUb) is Parkin activator. Interestingly, two sets of NMR signals were observed in HSQC spectrum of pUb. The major form has a closely similar conformation to the wild type. On the other hand, the minor form has entirely different hydrogen bonding patterns at b-sheet region, in which b5-strand has retracted into the ubiquitin core region by two amino acid residues. The retracted minor conformation provides different interaction surface on the ubiquitin hydrophobic patch from that of the major one. Here, we report the analysis of conformational fluctuation of pUb using high-pressure NMR spectroscopy. Our results indicate that pressure-induced chemical shifts were markedly different at the b-sheet and a-helix regions between the major and minor ones, indicating that pressure-induced changes in hydrogen bond length and torsion angles are different at the b-sheet region.
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