Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 23, Issue 7, Pages 1182-1190Publisher
SPRINGER
DOI: 10.1007/s13361-012-0379-x
Keywords
Photodissociation; Charge tags; Peptide ions
Funding
- National Science Foundation [CHE-1012855, CHE-0911454]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1012855] Funding Source: National Science Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0911454] Funding Source: National Science Foundation
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Tris(2,4,6-trimethoxyphenyl) phosphonium acetyl (TMPP-Ac) was previously introduced to improve the mass spectrometric sequence analysis of peptides by fixing a permanent charge at the N-termini. However, peptides containing arginine residues did not fragment efficiently after TMPP-Ac modification. In this work, we combine charge derivatization with photodissociation. The fragmentation of TMPP-derivatized peptides is greatly improved and a series of N-terminal fragments is generated with complete sequence information. Arginine has a special effect on the fragmentation of the TMPP tagged peptides when it is the N-terminal peptide residue. Theoretical and experimental results suggest that this is due to hydrogen transfer from the charged N-terminus to the hydrogen-deficient peptide sequence.
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