Differential Ion Mobility Separations of Peptides with Resolving Power Exceeding 50 | Zendy

Alexandre A. Shvartsburg | Zendy; Keqi Tang | Zendy; Richard Smith | Zendy

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Differential Ion Mobility Separations of Peptides with Resolving Power Exceeding 50

Author(s) -

Alexandre A. Shvartsburg,

Keqi Tang,

Richard Smith

Publication year - 2009

Publication title -

analytical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.117

H-Index - 332

eISSN - 1520-6882

pISSN - 0003-2700

DOI - 10.1021/ac902133n

Subject(s) - chemistry , ion mobility spectrometry , ion , analytical chemistry (journal) , fractionation , resolution (logic) , chromatography , electric field , mass spectrometry , peptide , helium , organic chemistry , biochemistry , physics , quantum mechanics , artificial intelligence , computer science

Differential ion mobility spectrometry (IMS) or field asymmetric waveform IMS (FAIMS) separates gas-phase ions by mobility differences with respect to the electric field intensity. A major emerging FAIMS application is the fractionation of proteolytic digests. Using a planar FAIMS unit with helium/nitrogen mixtures, we have increased FAIMS resolving powers for peptide analyses from the prior maximum of approximately 20-30 to approximately 50-70. The resolution improved nearly 3-fold, allowing, in particular, separation of previously unresolved conformers.

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