Changes
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<p><strong>Colclusion</strong></p>
<p>Chemical probe to catch N-phosphorylated protein have been developing and it is attractive way to figure out biological function of N-phosphorylation. I conducted reaearch about finding chemical probe of pLys and pAsp(althought it is not N-phosphorylation, it is also not stable) using antibody. This chemical approach to unstable phosphorylation is quite attractive but not easy. So I proposed another way to investigate the function of unstable non-canonical amino acids by developing tRNA and aminoacyl tRNA synthetase. If we can manage N-phosphorylated protein in organism, then it would be much easier, even after developing chemical probe for those amino acids, to conduct biological assay.</p>
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<p>P. G. Besant, P. V. Attwood, M. J. Piggott. Current Protein & Peptide Science, Volume 10 , Issue 6 , 2009, Focus on Phosphoarginine and Phospholysine</p>
<p>Lei Wang, Ansgar Brock, Brad Herberich, Peter G. Schultz, Science, Volume 292, 20 April 2001, Expanding the Genetic Code of Escherichia coli</p>