Sunday, March 4, 2012, 9:00 am - 12:00 pm.  Tuition is $100.  

Organizer:  Donald F. Hunt (University of Virginia) 

Course Description
Electron transfer dissociation mass spectrometry is a break-though technology for sequencing post-translationally modified peptides and proteins. In this technique, radical anions of polyaromatic hydrocarbons (fluoranthene and azulene) are employed to transfer electrons to the carbonyl group in the polyamide backbone of multiply charged peptides generated by electrospray ionization. Capture of an electron into the peptide backbone reduces the positive charge on the ion by one, and forms a carbonyl radical anion that then abstracts a proton from a nearby protonated amino group. The resulting carbonyl radical triggers cleavage of the adjacent nitrogen-carbon bond to produce fragments of type c’ and z•.   

The purpose of the workshop is to provide instruction on how to manually interpret peptide ETD mass spectra. In the morning session (9 am to 12 pm) we will begin with an overview of the technique and present examples that illustrate how superior this approach is to classical collision activated dissociation MS/MS.  Following a lengthy tutorial about ion structures, fragmentation pathways, predictable changes in fragment ion isotope patterns, etc., we will outline a general approach for the manual interpretation of peptide ETD spectra and solve the sequence of several post-translationally modified peptides. Homework problems will be assigned for the afternoon session from 12:00 pm – 4:15 pm. We will then reconvene, go over the assigned problems, and hopefully tackle interpretation of several spectra recorded on more highly charged (and larger) peptides (+4 and +5).   

A packet of lecture notes and handouts will be provided.  Attendees should bring an inexpensive calculator, pad of paper, and a small ruler.

Level:  Intermediate to advanced.

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