ArticleJournal of the American Society for Mass Spectrometry2010
Effect of N-terminal glutamic acid and glutamine on fragmentation of peptide ions.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Proteomic Analysis of S-Palmitoylated Proteins in Ocular Lens Reveals Palmitoylation of AQP5 and MP20.Investigative ophthalmology & visual science · 2018Article
- Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry.Analytical chemistry · 2017Article
- The Art of Destruction: Optimizing Collision Energies in Quadrupole-Time of Flight (Q-TOF) Instruments for Glycopeptide-Based Glycoproteomics.Journal of the American Society for Mass Spectrometry · 2016Article
- Article
- Disfavoring macrocycle b fragments by constraining torsional freedom: the "twisted" case of QWFGLM b6.Journal of the American Society for Mass Spectrometry · 2012Article
- Investigation of VUV Photodissociation Propensities Using Peptide Libraries.International journal of mass spectrometry · 2011Article
- Mass spectrometry analysis of 2-nitrophenylhydrazine carboxy derivatized peptides.Journal of the American Society for Mass Spectrometry · 2011Article
- Charge states of y ions in the collision-induced dissociation of doubly charged tryptic peptide ions.Journal of the American Society for Mass Spectrometry · 2011Article
- Effect of the identity of Xaa on the fragmentation modes of doubly-protonated Ala-Ala-Xaa-Ala-Ala-Ala-Arg.Journal of the American Society for Mass Spectrometry · 2011Article
- Lessons in de novo peptide sequencing by tandem mass spectrometry.Mass spectrometry reviewsReview
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A prominent dissociation path for electrospray generated tryptic peptide ions is the dissociation of the peptide bond linking the second and third residues from the amino-terminus. The formation of the resulting b(2) and y(n-2) fragments has been rationalized by specific facile mechanisms. An examination of spectral libraries shows that this path predominates in diprotonated peptides composed of 12 or fewer residues, with the notable exception of peptides containing glutamine or glutamic acid at the N-terminus. To elucidate the mechanism by which these amino acids affect peptide fragmentation, we synthesized peptides of varying size and composition and examined their MS/MS spectra as a function of collision voltage in a triple quadrupole mass spectrometer. Loss of water from N-terminal glutamic acid and glutamine is observed at a lower voltage than any other fragmentation, leading to cyclization of the terminal residue. This cyclization results in the conversion of the terminal amine group to an imide, which has a lower proton affinity. As a result, the second proton is not localized at the N-terminus but is readily transferred to other sites, leading to fragmentation near the center of the peptide. Further confirmation was obtained by examining peptides with N-terminal pyroglutamic acid and N-acetyl peptides. Peptides with N-terminal proline maintain the trend of forming b(2) and y(n-2) because their ring contains an imine rather than imide and has sufficient proton affinity to retain the proton at the N-terminus.
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