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Site-Specific Radical Directed Dissociation of Peptides at Phosphorylated Residues
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Section:Abstract
Site-specific fragmentation of peptides at phosphorylated serine or threonine residues is demonstrated. This radical directed cleavage is accomplished by a two-step procedure. First the phosphate is replaced with naphthalenethiol using well established Michael Addition chemistry. Second, the modified peptide is electrosprayed and subjected to irradiation at 266 nm. Absorption at naphthalene causes homolytic cleavage of the connecting carbon−sulfur bond yielding a radical in the β-position. Subsequent rearrangement cleaves the peptide backbone yielding a d-type fragment. This chemistry is generally applicable as demonstrated by experiments with several different peptides. Assignment of phosphorylation sites is greatly facilitated by this approach, particularly for peptides containing multiple serine or threonine residues.
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This article has been cited by 8 ACS Journal articles (5 most recent appear below).
Facile Identification of Phosphorylation Sites in Peptides by Radical Directed Dissociation
Jolene K Diedrich and Ryan R JulianAnalytical Chemistry 0 (ja),Facile Identification of Phosphorylation Sites in Peptides by Radical Directed Dissociation
Jolene K Diedrich and Ryan R JulianAnalytical Chemistry 0 (ja),Identification of phosphorylation sites is of interest due to their importance in protein regulation. However the identification of the exact sites of this modification is not always easily obtained due to the dynamic nature of phosphorylation and the ...
Enhancement of Ultraviolet Photodissociation Efficiencies through Attachment of Aromatic Chromophores
Lisa Vasicek and Jennifer S. BrodbeltAnalytical Chemistry2010 82 (22), 9441-9446Enhancement of Ultraviolet Photodissociation Efficiencies through Attachment of Aromatic Chromophores
Lisa Vasicek and Jennifer S. BrodbeltAnalytical Chemistry2010 82 (22), 9441-9446Two N-terminal derivatization reagents containing aromatic chromophores, 4-sulfophenyl isothiocyanate (SPITC) and 4-methylphosphonophenyl isothiocyanate (PPITC), were used to increase the dissociation efficiencies of peptides upon ultraviolet ...
Study of Highly Selective and Efficient Thiol Derivatization Using Selenium Reagents by Mass Spectrometry
Kehua Xu, Yun Zhang, Bo Tang, Julia Laskin, Patrick J. Roach and Hao ChenAnalytical Chemistry2010 82 (16), 6926-6932Study of Highly Selective and Efficient Thiol Derivatization Using Selenium Reagents by Mass Spectrometry
Kehua Xu, Yun Zhang, Bo Tang, Julia Laskin, Patrick J. Roach and Hao ChenAnalytical Chemistry2010 82 (16), 6926-6932This paper reports a systemic mass spectrometry (MS) investigation of a novel strategy for labeling biological thiols, involving the cleavage of the Se−N bond by thiol to form a new Se−S bond. Our data show that the reaction is highly selective, rapid, ...
Preferential Cleavage of N−N Hydrazone Bonds for Sequencing Bis-arylhydrazone Conjugated Peptides by Electron Transfer Dissociation
Myles W. Gardner and Jennifer S. BrodbeltAnalytical Chemistry2010 82 (13), 5751-5759Preferential Cleavage of N−N Hydrazone Bonds for Sequencing Bis-arylhydrazone Conjugated Peptides by Electron Transfer Dissociation
Myles W. Gardner and Jennifer S. BrodbeltAnalytical Chemistry2010 82 (13), 5751-5759Electron transfer dissociation (ETD) was used to sequence bis-arylhydrazone (BAH)-cross-linked peptides through preferential cleavage of the hydrazone bond. On average, 58% of the observed ETD product ion abundance was accounted for by fragment ions due ...
Site-Selective Fragmentation of Peptides and Proteins at Quinone-Modified Cysteine Residues Investigated by ESI-MS
Jolene K. Diedrich and Ryan R. JulianAnalytical Chemistry2010 82 (10), 4006-4014Site-Selective Fragmentation of Peptides and Proteins at Quinone-Modified Cysteine Residues Investigated by ESI-MS
Jolene K. Diedrich and Ryan R. JulianAnalytical Chemistry2010 82 (10), 4006-4014Described herein are several unique analytical applications utilizing mass spectrometry and the selective modification of the free thiol form of cysteine in both peptides and proteins by various quinones. This simple modification can be used to quantify ...
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History
- Published In Issue September 17, 2008
- Article ASAPAugust 19, 2008
- Received: April 01, 2008
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