Mass spectrometry, specifically tandem mass spectrometry (MS2 spectrometry), is a well-used analytical technique. It is widely used experimentally and has the the focus of numerous computational studies. The MS2 technique allows for a careful mass selection followed by collisional excitation that leads to fragmentation of the selected species. The resultant spectrum is useful in sequence determination. However, the presence of post-translational modifications (PTM) to the peptides, such as alkylation, methylation and sulfonation, complicate the identification of primary sequences largely due to unintuitive fragmentation pathways. Computational studies of species that have PTMs are just beginning to be reported in the literature. In this work, we employ molecular dynamics simulations of serine and its <i>O</i>-sulfonated form to examine how PTM affects MS2 fragmentation events. Results will be used to provide atomistic details regarding the mechanism and pathways of fragmentation. We will explore what influence the PTM has on the preferred fragmentation products, as well as their mechanisms.

Simulations of serine vs. sulfoserine: Mass spectra and fragmentation pathways during CID

2019 Fall National Meeting

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