【摘 要】
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We have recently demonstrated that free radical initiated peptide sequencing mass spectrometry (FRIPS MS) utilizing the remarkable thermochemical stability of (
【机 构】
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DepartmentofChemistry,SogangUniversity,Seoul,Korea
【出 处】
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The 9th Asian Biophysics Association Symposium (ABA2015)(第九届
论文部分内容阅读
We have recently demonstrated that free radical initiated peptide sequencing mass spectrometry (FRIPS MS) utilizing the remarkable thermochemical stability of (2,2,6,6-Tetramethyl-piperidin-1-yl)oxyl (TEMPO) is an attractive radical-driven peptide fragmentation mass spectrometry tool.o-TEMPO-Bz-C(O)-peptides could be produced through a simple NHS peptide conjugation reaction.The produced o-TEMPO-Bz-C(O)-peptide generally undergoes facile homolytic cleavage at the bond between the benzylic carbon and the oxygen of the TEMPO moiety in o-TEMPO-Bz-C(O)-peptide.Then, the generated radical-species have been shown to produce extensive radical-based peptide fragmentations upon the additional collisional activation.Since its initial development, a variety of usages of this method have been shown as efforts to make this tool more usable in practical proteomics research;for example, guanidination approach, disulfide mapping ability, de-novo sequencing, middle-down possiblity, and so on.In the symposium, further details that shed light on its potential as another future proteomics tool will be given.
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