Optimization of Electron
Transfer Dissociation via
Informed Selection of Reagents and Operating Parameters
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Abstract
Electron transfer dissociation (ETD) has improved the
mass spectrometric
analysis of proteins and peptides with labile post-translational modifications
and larger intact masses. Here, the parameters governing the reaction
rate of ETD are examined experimentally. Currently, due to reagent
injection and isolation events as well as longer reaction times, ETD
spectra require significantly more time to acquire than collision-induced
dissociation (CID) spectra (>100 ms), resulting in a trade-off
in
the dynamic range of tandem MS analyses when ETD-based methods are
compared to CID-based methods. Through fine adjustment of reaction
parameters and the selection of reagents with optimal characteristics,
we demonstrate a drastic reduction in the time taken per ETD event.
In fact, ETD can be performed with optimal efficiency in nearly the
same time as CID at low precursor charge state (<i>z</i> = +3) and becomes faster at higher charge state (<i>z</i> > +3)