| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Outline of Final Research Achievements |
The conventional NMR approach for structure determination so far reveals atomic coordinates of the most stable conformation of a protein, the so-called “native state”. Despite significant progress in our knowledge about the basic folded conformation of proteins, high-Gibbs free energy states of proteins are poorly understood. Here, we investigate the structure and backbone dynamics of locally disordered state of ubiquitin using high pressure NMR spectroscopy. We carried out NMR signal assignments, the collection of structural information based on chemical shifts, NOE, and paramagnetic relaxation enhancements (PRE). We also performed 15N spin relaxation experiments (T1, T2, hNOE). More than 1000 NOE- and PRE-based distance constraints and 42 torsion angle constraints were used for structure calculation of the locally disordered state. High-pressure NMR spectroscopy provides snapshots of fluctuating ubiquitin structure at atomic resolution.
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