ArticleJournal of the American Society for Mass Spectrometry2008
The role of phosphorylated residues in peptide-peptide noncovalent complexes formation.
Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Noncovalently Associated Peptides Observed during Liquid Chromatography-Mass Spectrometry and Their Effect on Cross-Link Analyses.Analytical chemistry · 2019Article
- Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer.International journal of mass spectrometry · 2014Article
- How adenylate cyclase choreographs the pas de deux of the receptors heteromerization dance.Neuroscience · 2013Article
- MALDI/post ionization-ion mobility mass spectrometry of noncovalent complexes of dopamine receptors' epitopes.Journal of proteome research · 2013Article
- Competition between covalent and noncovalent bond cleavages in dissociation of phosphopeptide-amine complexes.Physical chemistry chemical physics : PCCP · 2011Article
- Dipole-guided electron capture causes abnormal dissociations of phosphorylated pentapeptides.Journal of the American Society for Mass Spectrometry · 2011Article
- Interactions between intracellular domains as key determinants of the quaternary structure and function of receptor heteromers.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Electrospray mass spectrometry (ESI-MS) has become the tool of choice for the study of noncovalent complexes. Our previous work has highlighted the role of phosphorylated amino acid residues in the formation of noncovalent complexes through electrostatic interaction with arginine residues' guanidinium groups. In this study, we employ tandem mass spectrometry to investigate the gas-phase stability and dissociation pathways of these noncovalent complexes. The only difference in the three phosphopeptides tested is the nature of the phosphorylated amino acid residue. In addition the absence of acidic residues and an amidated carboxyl terminus insured that the only negative charge came from the phosphate, which allowed for the comparison of the noncovalent bond between arginine residues and each of the different phosphorylated residues. Dissociation curves were generated by plotting noncovalent complex ion intensities as a function of the nominal energy given to the noncovalent complex ion before entering the collision cell. These results showed that noncovalent complexes formed with phosphorylated tyrosine were the most stable, followed by serine and threonine, which had similar stability.
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