2014 Fiscal Year Final Research Report
NMR approach and prediction for the residual structures in the intrinsically disordered proteins
| Project/Area Number |
23590049
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Teikyo Heisei University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
GOTO Yuji 大阪大学, 蛋白質研究所, 教授 (40153770)
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| Project Period (FY) |
2011-04-28 – 2015-03-31
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| Keywords | 核磁気共鳴 / 天然変性蛋白質 / 残存構造 / ２次構造 / 緩和時間 / 化学シフト / 揺らぎ構造 / ウイルス |
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| Outline of Final Research Achievements |
Residual and ensemble structures in intrinsically disordered proteins can be directly related to their functions. For alpha-synuclein, the N- and C-terminal domains were slightly more protected from the amide-proton exchange than the other regions monitored by CLEANEX-PM. Chemical shift studies and delta2d analyses were powerful tools to figure out the minor populations of the residual alpha- and beta-structures for the measles virus C-terminal domain Ntail of nucleoprotein. The amounts of residual structures in both proteins were very small.
HIV-1 p17 matrix protein and p24 capsid N-terminal domain fold in the physiological condition as globular proteins, although two proteins were predicted to be 50% unfolded based on the sequence. The order-parameter studies on p17 revealed that the more flexibility was included in helix 5 than in the other helices. For p24, the long-range effects by the addition of the unnecessary tag on the dynamics structures were observed at helices 4 and 6.
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| Free Research Field |
物理系薬学
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