Development of the new method for dynamics analysis in large molecular protein-protein complex using nuclear magnetic resonance
Project/Area Number |
25840021
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
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Research Institution | Nagoya University |
Principal Investigator |
MIYANOIRI Yohei 名古屋大学, 理学(系)研究科(研究院), 特任助教 (80547521)
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Project Period (FY) |
2013-04-01 – 2015-03-31
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Project Status |
Completed (Fiscal Year 2014)
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Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2014: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | NMR / 蛋白質動態 |
Outline of Final Research Achievements |
To elucidate the dynamic properties of GroEL-ES protein complexs, We have developed new relaxation optimized Stereo-Array Isotope labelling (SAIL) method. Using new relaxation optimized SAIL amino acids, we could succeed in observing well-separeted aromatic, aliphatic and methyl CH signals for GroEL-ES complex. And we could detect the changes in structural flactuations in several amino acid s in GroEL and GroES upon forming GroEL-ES complex. These dynamics may play an important role for cotrolling a biological function of GroEL-ES complex. Our new SAIL NMR method will be useful for structural dynamics study in many macromolecular protein complexes.
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Report
(3 results)
Research Products
(12 results)
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[Journal Article] Expression and purification of a GRAS domain of SLR1, the rice DELLA protein.2014
Author(s)
Sato T, Miyanoiri Y, Takeda M, Naoe Y, Mitani R, Hirano K, Takehara S, Kainosho M, Matsuoka M, Ueguchi-Tanaka M, Kato H
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Journal Title
Protein Expr Purif.
Volume: 95
Pages: 248-258
DOI
Related Report
Peer Reviewed / Open Access
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