Journal of the American Society for Mass Spectrometry

, Volume 20, Issue 4, pp 618–624

What is the structure of b2 ions generated from doubly protonated tryptic peptides?

Articles

DOI: 10.1016/j.jasms.2008.11.021

Cite this article as:
Bythell, B.J., Somogyi, Á. & Paizs, B. J Am Soc Mass Spectrom (2009) 20: 618. doi:10.1016/j.jasms.2008.11.021

Abstract

A recent statistical study (Savitski, M. M.; Falth, M.; Eva Fung, Y. M.; Adams, C. M.; Zubarev, R. A. J. Am. Soc. for Mass Spectrom. doi: 10.1016/j.jasms.2008.08.003) of a large spectral database indicated that the product ion spectra of doubly protonated tryptic peptides fall into two distinct classes. The main factor distinguishing the two classes is the relative abundance of the yN-2 fragment: for Class I spectra yN-2 is the most abundant y fragment while for Class II other y ions dominate the corresponding spectra. To explain the dominance of yN-2 for Class I spectra formation of a nontraditional b2 ion with a diketopiperazine (6-membered cyclic peptide) rather than an oxazolone structure was proposed. Here we present evidence from tandem mass spectrometry, hydrogen/deuterium exchange, and density functional calculations that do not support this proposal. Namely, that CID of doubly protonated YIGSR, YGGFLR, and YIYGSFK produce Class I product ion spectra, yet the b2 fragment is shown to have the traditional oxazolone structure.

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© American Society for Mass Spectrometry 2009

Authors and Affiliations

  1. 1.Department of Molecular BiophysicsGerman Cancer Research Centr (DKFZ)HeidelbergGermany
  2. 2.Department of ChemistryUniversity of ArizonaTucsonUSA