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Negative ion cleavages of (M-H)- anions of peptides. Part 3. Post-translational modifications
Journal article   Peer reviewed

Negative ion cleavages of (M-H)- anions of peptides. Part 3. Post-translational modifications

Tianfang Wang, T T Nha Tran, Hayley J Andrewazza, Daniel Bilusich, Craig S Brinkworth and John H Bowie
Mass Spectrometry Reviews, Vol.37(1), pp.3-21
2018
url
https://doi.org/10.1002/mas.21501View
Published Version

Abstract

negative-ion electrospray mass spectrometry quantum mechanical hydrogen tunneling peptides
It is now 25 years since we commenced the study of the negative-ion fragmentations of peptides and we have recently concluded this research with investigations of the negative-ion chemistry of most post-translational functional groups. Our first negative-ion peptide review (Bowie, Brinkworth, & Dua, 2002) dealt with the characteristic backbone fragmentations and side-chain cleavages from (M-H)- ions of underivatized peptides, while the second (Bilusich & Bowie, 2009) included negative-ion backbone cleavages for Ser and Cys and some initial data on some post-translational groups including disulfides. This third and final review provides a brief summary of the major backbone and side chain cleavages outlined before (Bowie, Brinkworth, & Dua, 2002) and describes the quantum mechanical hydrogen tunneling associated with some proton transfers in enolate anion/enolate systems. The review then describes, in more depth, the negative-ion cleavages of the post-translational groups Kyn, isoAsp, pyroglu, disulfides, phosphates, and sulfates. Particular emphasis is devoted to disulfides (both intra- and intermolecular) and phosphates because of the extensive and spectacular anion chemistry shown by these groups. © 2016 Wiley Periodicals, Inc. Mass Spec Rev

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