Proteomics

Dataset Information

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Ion mobility tandem mass spectrometry enhances performance of bottom-up proteomics


ABSTRACT: We describe a novel method utilizing ion mobility-based concentration of peptide fragment ions on a qTOF mass spectrometer improving the sensitivity of bottom-up proteomics by up to 10-fold. This enabled the identification of 7,500 human proteins within one day and 8,600 phosphorylation sites within 5h of LC-MS/MS time. The method also proved powerful for multiplexed quantification experiments exemplified by the chemoproteomic interaction analysis of HDACs with Trichostatin A.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Spleen, Testis, Ovary, Prostate Gland, Lung, Liver, Kidney

SUBMITTER: Hannes Hahne  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD000863 | Pride | 2015-08-18

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
130826_GradientTime_15min_R1.mz5 Other
130826_GradientTime_15min_R2.mz5 Other
130826_GradientTime_15min_R3.mz5 Other
130826_GradientTime_30min_R1.mz5 Other
130826_GradientTime_30min_R2.mz5 Other
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Publications


One of the limiting factors in determining the sensitivity of tandem mass spectrometry using hybrid quadrupole orthogonal acceleration time-of-flight instruments is the duty cycle of the orthogonal ion injection system. As a consequence, only a fraction of the generated fragment ion beam is collected by the time-of-flight analyzer. Here we describe a method utilizing postfragmentation ion mobility spectrometry of peptide fragment ions in conjunction with mobility time synchronized orthogonal ion  ...[more]

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