title: 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.
authors.affiliation: Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, United States. alexandre.shvartsburg@pnl.gov
authors.forename: Alexandre A
authors.initials: AA
authors.lastname: Shvartsburg
authors.forename: Yupeng
authors.initials: Y
authors.lastname: Zheng
authors.forename: Richard D
authors.initials: RD
authors.lastname: Smith
authors.forename: Neil L
authors.initials: NL
authors.lastname: Kelleher
mesh_terms: D000107:Acetylation; D006371:Helium / Q000737:chemistry; D006657:Histones / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry; D007477:Ions / Q000737:chemistry*; D013058:Mass Spectrometry; D009584:Nitrogen / Q000737:chemistry; D010455:Peptides / Q000032:analysis
chemical_list: D006657:Histones; D007477:Ions; D010455:Peptides; D006371:Helium; D006859:Hydrogen; D009584:Nitrogen