I thought for sure I'd already posted this paper, but I can't find it!
Either way, this is worth talking about (again?). The basic idea is that if you really think about your populations of intact proteoforms in your samples in terms of:
1) What proteoforms you can actually detect (don't worry too much about Titin for now)
2) How much easier it is to identify smaller protein/proteoforms in most experiments (small proteins may need no microscans or scan averaging, while larger ones will need more)
3) How FAIMS compensation voltages can help enrich proteins of certain sizes (this was new to me and why I really like this paper)
4) How chromatography can also do some of #3
You can get some dramatic increases in identification rates versus both systems without FAIMS and systems where less FAIMS method optimization has been employed.
How much more?
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