Ultrasensitive identification of localization variants of modified peptides using ion mobility spectrometry.

ABSTRACT: Localization of the modification sites on peptides is challenging, particularly when multiple modifications or mixtures of localization isomers (variants) are involved. Such variants commonly coelute in liquid chromatography and may be undistinguishable in tandem mass spectrometry (MS/MS) for lack of unique fragments. Here, we have resolved the variants of singly and doubly phosphorylated peptides employing drift tube ion mobility spectrometry (IMS) coupled to time-of-flight mass spectrometry. Even with a moderate IMS resolving power of ∼80-100, substantial separation was achieved for both 2+ and 3+ ions normally generated by electrospray ionization, including for the variants indistinguishable by MS/MS. Variants often exhibit a distribution of 3-D conformers, which can be adjusted for opt

SUBMITTER: Ibrahim YM 

PROVIDER: S-EPMC3136632 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature