| Budget Amount *help |
¥17,290,000 (Direct Cost: ¥13,300,000、Indirect Cost: ¥3,990,000)
Fiscal Year 2021: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
Fiscal Year 2020: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2019: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2018: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
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| Outline of Final Research Achievements |
In this study, we showed that the enzymatic activity of a rhomboid protease is regulated by the alkyl chain length and the properties of hydrophilic head groups of solubilized detergents. And it was found that the enzymatic activity is inversely correlated with the thermal stability of the molecule, which inferred that the internal dynamics of the rhomboid protease affects the enzymatic activities. Using microbial rhodopsin derived from thermophilic eubacteria, we performed a systematic analysis of the thermal stability in different membrane mimetics including bicelles and nanodiscs, which provides us a useful index of choices of membrane environments for functional and structural analyses of membrane proteins. Furthermore, NMR analysis of the rhodopsin in different environments revealed that the environmental difference induces local structural changes that affect the thermal stability of the molecule.
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