Separation of a Set of Peptide Sequence Isomers Using Differential Ion Mobility Spectrometry

AA Shvartsburg; Andrew Creese; RD Smith; Helen Cooper

doi:10.1021/ac201640d

Separation of a Set of Peptide Sequence Isomers Using Differential Ion Mobility Spectrometry

AA Shvartsburg, Andrew Creese, RD Smith, Helen Cooper

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Abstract

Protein identification in bottom-up proteomics requires disentangling isomers of proteolytic peptides, a major class of which are sequence inversions. Their separation using ion mobility spectrometry (IMS) has been limited to isomeric pairs. Here we demonstrate baseline separation of all seven 8-mer tryptic peptide isomers using differential IMS. Evaluation of peak capacity implies that even larger libraries should be resolved for heavier peptides with higher charge states.

Original language	English
Pages (from-to)	6918-6923
Number of pages	6
Journal	Analytical Chemistry
Volume	83
Issue number	18
DOIs	https://doi.org/10.1021/ac201640d
Publication status	Published - 1 Sept 2011

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title = "Separation of a Set of Peptide Sequence Isomers Using Differential Ion Mobility Spectrometry",

abstract = "Protein identification in bottom-up proteomics requires disentangling isomers of proteolytic peptides, a major class of which are sequence inversions. Their separation using ion mobility spectrometry (IMS) has been limited to isomeric pairs. Here we demonstrate baseline separation of all seven 8-mer tryptic peptide isomers using differential IMS. Evaluation of peak capacity implies that even larger libraries should be resolved for heavier peptides with higher charge states.",

author = "AA Shvartsburg and Andrew Creese and RD Smith and Helen Cooper",

year = "2011",

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AU - Shvartsburg, AA

AU - Creese, Andrew

AU - Smith, RD

AU - Cooper, Helen

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N2 - Protein identification in bottom-up proteomics requires disentangling isomers of proteolytic peptides, a major class of which are sequence inversions. Their separation using ion mobility spectrometry (IMS) has been limited to isomeric pairs. Here we demonstrate baseline separation of all seven 8-mer tryptic peptide isomers using differential IMS. Evaluation of peak capacity implies that even larger libraries should be resolved for heavier peptides with higher charge states.

AB - Protein identification in bottom-up proteomics requires disentangling isomers of proteolytic peptides, a major class of which are sequence inversions. Their separation using ion mobility spectrometry (IMS) has been limited to isomeric pairs. Here we demonstrate baseline separation of all seven 8-mer tryptic peptide isomers using differential IMS. Evaluation of peak capacity implies that even larger libraries should be resolved for heavier peptides with higher charge states.

U2 - 10.1021/ac201640d

DO - 10.1021/ac201640d

M3 - Article

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SN - 1520-6882

VL - 83

SP - 6918

EP - 6923

JO - Analytical Chemistry

JF - Analytical Chemistry

IS - 18

ER -

Separation of a Set of Peptide Sequence Isomers Using Differential Ion Mobility Spectrometry

Abstract

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