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- E-ISSN 2093-8950
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- P-ISSN2233-4203
- E-ISSN2093-8950
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Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)- Peptides
Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2013, v.4 no.4, pp.71-74
https://doi.org/10.5478/MSL.2013.4.4.71
(Sogang University)
(Sogang University)
(Sogang University)
(Diatech Korea Co. Ltd.)
(Sogang University)
(Sogang University)
(Sogang University)
(Sogang University)
(Diatech Korea Co. Ltd.)
(Sogang University)
(Sogang University)
Jeon,
A., Lee,
J. H., Kwon,
H. S., Park,
H. S., Bong Jin,
M., &
Oh,
H.
B.
(2013). Charge-Directed Peptide Backbone Dissociations of o-TEMPO-Bz-C(O)- Peptides. Mass Spectrometry Letters, 4(4), 71-74, https://doi.org/10.5478/MSL.2013.4.4.71
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Abstract
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.
- keywords
- Charge-directed dissociations, Peptide, Free radical initiated peptide sequencing, Mobile proton model, Radical chemistry
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- Submission Date
- 2013-12-01
- Revised Date
- 2013-12-02
- Accepted Date
- 2013-12-02
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