| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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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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