Abstract

Poster Presentations

Day 1, May 15（Wed.）　　Room P (Multi-purpose Hall)

1P-10　　PDF

Fragmentation Influenced by Mobile Proton on Side Chain of Arginine

(¹Hiroshima Univ., ²Hiroshima Univ.)
^oWataru Fukuda¹, Megumi Furumitsu², Kazuyoshi Ukena², Shunsuke Izumi¹, Kazumi Saikusa¹

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.