2012 Fiscal Year Final Research Report
Development of new method in structural analysis for larger proteinsusing nuclear magnetic resonances
Project/Area Number |
23770111
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
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Research Institution | Nagoya University |
Principal Investigator |
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Project Period (FY) |
2011 – 2012
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Keywords | NMR / 蛋白質 |
Research Abstract |
We have developed new SAIL aromatic amino acids which are optimized relaxation properties in aromatic ring and successfully observed extremely well-separated aromatic CH cross peaks in TROSY experiment, even for an 82kDa E. colimalate synthase G (MSG) protein. Using our new SAILaromatic CH TROSY method, we could clearly assign many NOE signals among aromatic CH, methyl and amide signals which are very important for determining the precise structure of large molecular proteins.
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