Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)-Peptides
In the present study, we report that the charge-directed (assisted) peptide dissociation products, such as b- and y-type peptidebackbone fragments, were the major products in MS/MS and MS3 applications of some o-TEMPO-Bz-C(O)-peptide ions, whileradical-driven dissociation products, such as a/x and c...
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Published in | Mass spectrometry letters Vol. 4; no. 4; pp. 71 - 74 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
한국질량분석학회
01.12.2013
사단법인 한국질량분석학회 |
Subjects | |
Online Access | Get full text |
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Summary: | In the present study, we report that the charge-directed (assisted) peptide dissociation products, such as b- and y-type peptidebackbone fragments, were the major products in MS/MS and MS3 applications of some o-TEMPO-Bz-C(O)-peptide ions, whileradical-driven dissociation products, such as a/x and c/z-type fragments, were previously shown to be the major products in the freeradical initiated peptide sequencing mass spectrometry (FRIPS MS). Those o-TEMPO-Bz-C(O)-peptides share a common feature intheir sequences, that is, the peptides do not include an arginine residue that has the highest proton affinity among free amino acids.
The appearance of b- and y-type fragments as major products in FRIPS MS can be understood in terms of the so-called “mobile-protonmodel”. When the proton is highly mobilized by the absence of arginine, the chare-directed peptide dissociation pathways appearto be more competitive than the radical-driven dissociation pathways, in our FRIPS experiments. KCI Citation Count: 1 |
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Bibliography: | G704-SER000003866.2013.4.4.003 |
ISSN: | 2233-4203 2093-8950 |
DOI: | 10.5478/MSL.2013.4.4.71 |