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Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry.


ABSTRACT: High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. Polyproline assumes an all-cis conformation-the PPI helix-in 1-propanol, and an all-trans conformation-the PPII helix-in aqueous solutions. Differentiation of these conformers may be achieved both through use of a cylindrical FAIMS device and a miniaturized ultrahigh field planar FAIMS device. Graphical Abstract ?.

SUBMITTER: Creese AJ 

PROVIDER: S-EPMC5088216 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry.

Creese Andrew J AJ   Cooper Helen J HJ  

Journal of the American Society for Mass Spectrometry 20161004 12


High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. Polyproline assumes an all-cis conformation-the PPI helix-in 1-propanol, and an all-trans conformation-the PPII helix-in aqueous solutions. Differentiation of these conformers may be achieved both thro  ...[more]

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