Electron Transfer Dissociation of iTRAQ Labeled Peptide Ions

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Peptide and protein quantification using iTRAQ with electron transfer dissociation.

Electron transfer dissociation (ETD) has become increasingly used in proteomic analyses due to its complementarity to collision-activated dissociation (CAD) and its ability to sequence peptides with post-translation modifications (PTMs). It was previously unknown, however, whether ETD would be compatible with a commonly employed quantification technique, isobaric tags for relative and absolute ...

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SHORT COMMUNICATION Electron Transfer Dissociation of Peptide Anions

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Radical-driven dissociation of odd-electron peptide radical ions produced in 157 nm photodissociation.

Odd-electron a + 1 radical ions generated in the 157 nm photodissociation of peptide ions were investigated in an ion trap mass spectrometer. To localize the radical, peptide backbone amide hydrogens were replaced with deuterium. When the resulting radical ions underwent hydrogen elimination, no H/D scrambling was obvious, suggesting that without collisional activation, the radical resides on t...

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Comprehensive Comparison of Collision Induced Dissociation and Electron Transfer Dissociation

Electron transfer dissociation (ETD) is a recently introduced mass spectrometric technique which has proven to be an excellent tool for the elucidation of labile post-translational modifications such as phosphorylation and O-GlcNAcylation of serine and threonine residues. However, unlike collision induced dissociation (CID), which has been studied for decades, the intricacies of ETD-based fragm...

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ژورنال

عنوان ژورنال: Journal of Proteome Research

سال: 2008

ISSN: 1535-3893,1535-3907

DOI: 10.1021/pr8001113