| Budget Amount *help |
¥178,620,000 (Direct Cost: ¥137,400,000、Indirect Cost: ¥41,220,000)
Fiscal Year 2013: ¥30,030,000 (Direct Cost: ¥23,100,000、Indirect Cost: ¥6,930,000)
Fiscal Year 2012: ¥30,030,000 (Direct Cost: ¥23,100,000、Indirect Cost: ¥6,930,000)
Fiscal Year 2011: ¥30,030,000 (Direct Cost: ¥23,100,000、Indirect Cost: ¥6,930,000)
Fiscal Year 2010: ¥30,030,000 (Direct Cost: ¥23,100,000、Indirect Cost: ¥6,930,000)
Fiscal Year 2009: ¥58,500,000 (Direct Cost: ¥45,000,000、Indirect Cost: ¥13,500,000)
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| Research Abstract |
In this study, we have developed novel methods to investigate flexible structure of intrinsically disordered proteins (IDPs) by small-angle X-ray scattering (SAXS) and molecular dynamics (MD) simulation (MD-SAXS) and by high-speed atomic force microscopy (AFM). In the MD-SAXS method, SAXS profile was calculated from the dynamic IDP model calculated considering complementary experimental data, and compared with experimental profile so that they are in agreement with the experimental data. In the high-speed AFM, a new method to reduce the noise level of the AFM device and a solution condition and supporting plate suitable for IDP observation have been developed. Reliability of the AFM has been assessed through the observation of PQBP-1 where NMR analysis went ahead for the identification of IDR. Based on these experiments, we have collaborated with a number of research group within this IDP research project in Japan and elucidated the structure-function relationship of various IDPs.
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