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Ion mobility separation of variant histone tails extending to the "middle-down" range.

ABSTRACT: 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.

SUBMITTER: Shvartsburg AA

PROVIDER: S-EPMC3353003 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Ion mobility separation of variant histone tails extending to the "middle-down" range.

Shvartsburg Alexandre A AA Zheng Yupeng Y Smith Richard D RD Kelleher Neil L NL

Analytical chemistry 20120503 10

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 protein ...[more]

PMID: 22559289

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