| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Outline of Final Research Achievements |
The specific aim of this study is to understand the mechanisms of protein folding in terms of physical chemistry, by quantitatively representing the structural and energetic characteristics of relevant species. Nonuniform chain collapse was observed in the early folding of staphylococcal nuclease by using ultrarapid mixing methods combined with fluorescence resonance energy transfer, indicating that specific interactions play a major role in forming early folding intermediates. A systematic study on urea-induced folding of apomyoglobin, using ultrarapid mixing methods, revealed that an ensemble of folding intermediates, which transiently accumulates during folding under strongly native conditions, is formed by the same kinetics as the equilibrium intermediate, which stably populated at equilibrium under moderately denaturing conditions, indicating that these molecular species consist of a single molecular species.
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