Hello everyone,
I am new to proteomics research and analyzing mass-spec data. I am trying to learn more about the theory/principle of TMT tagging (a type of isobaric labeling) coupled with LC-MS/MS spectrometry. I understand that each tag has a
1) protein binding group (amine reactive ONLY?) 2) reporter group (so we know the tag came from which sample?) 3) normalisation group (to ensure that each tag has same mass?) 4) cleavage group (so tag can be cleaved from the peptide?)
Did I get the purpose of all the four parts in the tag?
Also, what does it mean by 4-plex, 10-plex, n-plex tag? And why do the tags have different isotopes?
If I could have some clarity on the workflow of TMT tagging and how it leads to analysis, it would be really helpful. Also, if I could be provided with the document or a publication which explains each step of LC-MS/MS Tandem Mass Spectrometry, from sample prep, chromatography, to mass spec analysis, it would be really helpful. i tried reading many different articles but not all of them offer a clear, step-wise flow.
