| Budget Amount *help |
¥17,290,000 (Direct Cost: ¥13,300,000、Indirect Cost: ¥3,990,000)
Fiscal Year 2019: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2018: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2017: ¥8,060,000 (Direct Cost: ¥6,200,000、Indirect Cost: ¥1,860,000)
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| Outline of Final Research Achievements |
For seven-transmembrane proteins, we developed a statistical-mechanical theory enabling us to evaluate the thermostability from the structures, microscopic geometric characteristics. An originality of the theory is the incorporation of effects of translational, configurational entropy of hydrocarbon groups within the lipid bilayer. We found that mutating the residue at a position of NBW=3.39 (NBW is the BW number) to Lys or Arg leads to substantially higher thermostability for significantly many GPCRs of Class A in the inactive state. The structures of some of them were newly determined. TR and XR or RxR and HsBR (rhodopsins) are quite different in the thermostability despite their high sequence similarity. These experimental facts could be elucidated by our theory.
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