| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2009: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Research Abstract |
The determination of disulfide connectivity and conformation in a protein is essential for understanding the structural stability of the protein. However, no method for investigating them has been established. Here, a method for observing cross-bridge NOEs involving two b-protons of different cysteine residues has been developed. In a conventional uniformly isotope-labeled protein, the observation of such a NOE is difficult due to signal overlap and spin diffusion effect. In our approach, a protein whose protons are exclusively deuterated except for the two Cys's β-protons is employed, such that the connectivity and proton-proton distance can readily be determined.
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