Journal
ANALYTICAL CHEMISTRY
Volume 89, Issue 10, Pages 5461-5466Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.7b00379
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Funding
- VILLUM Foundation
- Lundbeck Foundation Postdoctoral Fellowship
- NIH COBRE [P30 GM110761]
- NSF CAREER [CHE-1552640]
- Lundbeck Foundation [R231-2016-3093, R192-2015-1363] Funding Source: researchfish
- Villum Fonden [00007292] Funding Source: researchfish
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1552640] Funding Source: National Science Foundation
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Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all functional PTMs are found on the N-terminal histone domains (tails) of similar to 50 residues protruding from the nucleosome core. Using high-definition differential ion mobility spectrometry (FAIMS) with electron transfer dissociation, we demonstrate rapid baseline gas-phase separation and identification of tails involving rnonomethylation, trimethylation, acetylation, or phosphorylation in biologically relevant positions. These are by far the largest variant peptides resolved by any method, some with PTM contributing just 0.25% to the mass. This opens the door to similar separations for intact proteins and in top-down proteomics.
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