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MALDI-CIDにおけるアルギニン側鎖を起点とするプロトン移動に伴うフラグメンテーション
Peptide sequencing by tandem mass spectrometry requires the information how peptide fragment in the gas phase. In general, the amide bonds cleavage in many peptides. However, enhanced cleavage (y9-35 ion) occurs at one site in melittin. In previous study, the masses of Ser18 and Arg22 were changed in the y9-35 ion, which resulted that Ser18 and Arg22 involved in the fragment mechanism of this ion. In this study, to understand the mechanism of y9-35 ion from melittin, we investigated the important amino acids except Ser18 and Arg22 in melittin for this cleavage. As a result, it was found that the basic amino acids on C-terminal were necessary to produce the y9-35 ion.