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

Alexandre A. Shvartsburg; Yupeng Zheng; Richard D. Smith; Neil L. Kelleher

doi:10.1021/ac300612y

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

Alexandre A. Shvartsburg^*, Yupeng Zheng, Richard D. Smith, Neil L. Kelleher

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

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.

Original language	English (US)
Pages (from-to)	4271-4276
Number of pages	6
Journal	Analytical Chemistry
Volume	84
Issue number	10
DOIs	https://doi.org/10.1021/ac300612y
State	Published - May 15 2012

ASJC Scopus subject areas

Analytical Chemistry

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10.1021/ac300612y

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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.",

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AU - Shvartsburg, Alexandre A.

AU - Zheng, Yupeng

AU - Smith, Richard D.

AU - Kelleher, Neil L.

PY - 2012/5/15

Y1 - 2012/5/15

N2 - 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.

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

Abstract

ASJC Scopus subject areas

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