4.8 Article

Ion Mobility Separation of Variant Histone Tails Extending to the Middle-Down Range

期刊

ANALYTICAL CHEMISTRY
卷 84, 期 10, 页码 4271-4276

出版社

AMER CHEMICAL SOC
DOI: 10.1021/ac300612y

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资金

  1. NCRR [RR18522]
  2. NIGMS [GM 067193-09, GM 103493-10]
  3. NCI [CA 155252]
  4. Northwestern University Physical Sciences Oncology Center [CA 143869]
  5. Chicago Biomedical Consortium
  6. Chicago Community Trust

向作者/读者索取更多资源

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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