Analysis of protein folding memory with modification of intramolecular chaperons and its application
| Project/Area Number |
24656501
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Kyoto University |
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Principal Investigator |
UEDA Mitsuyoshi 京都大学, 大学院・農学研究科, 教授 (90183201)
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| Project Period (FY) |
2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2012: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
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| Keywords | プロテインフォールディングメモリー / プロペプチド / 分子内シャペロン / カルボキシペプチダーゼ Y / 分子ディスプレイ / 活性化エネルギー / アンフィンセン理論 / 触媒効率 / カルボキシペプチダーゼY |
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| Research Abstract |
CPYs (carboxypeptidase Y) with mutated propeptides were successfully displayed on yeast cell surface, and the mature enzymes were purified by the selective cleavage of mutated propeptides. Measurement of the activity and kinetics of the displayed CPYs indicated that the propeptide mutation altered the catalytic efficiency of mCPY. Although the mature region of the wild -type and mutant CPYs had identical amino acid sequences, the mCPYs from the mutant proCPYs had higher catalytic efficiency than the wild-type. These results indicate that proteins with identical amino acid sequence can fold into isomeric proteins with micro-conformational changes through mutated intramolecular chaperones.
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Report
(2 results)
Research Products
(5 results)
