Journal
ANALYTICAL CHEMISTRY
Volume 84, Issue 10, Pages 4271-4276Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac300612y
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Funding
- NCRR [RR18522]
- NIGMS [GM 067193-09, GM 103493-10]
- NCI [CA 155252]
- Northwestern University Physical Sciences Oncology Center [CA 143869]
- Chicago Biomedical Consortium
- Chicago Community Trust
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Differential ion mobility spectrometry (FAIMS) can baseline-resolve multiple variants of post-translationally modified peptides extending to the 3-4 kDa range, which differ in the localization of a PTM as small as acetylation. Essentially orthogonal separations for different charge states expand the total peak capacity with the number of observed states that increases for longer polypeptides. This potentially enables resolving localization variants for yet larger peptides and even intact proteins.
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