Addressing the Repoducibility Aspect of LC-MS Based Protein Identification
Poster Aug 24, 2005
Jenny Samskog, Henrik Wadensten, and John Flensburg, GE Healthcare/ Amersham Biosciences AB, Uppsala, Sweden
IntroductionA major challenge in proteomics is the lack of reproducibility in protein identification experiments. In LCMS/MS analyses where the same sample is analyzed in replicates, many of the low abundant peptides that are successfully identified by searching a sequence collection with the MS/MS data are only identifiedin one or a few of the replicate runs.
By using the detection, matching, and visualization approach ofDeCyder™ MS were retention time, precursor mass, and the topology of the intensity profile is utilized in combination with the matching of tandem mass spectra, it is possible to achieve repeat analysis with a very high reproducibility.
By using the detection, matching, and visualization approach ofDeCyder™ MS were retention time, precursor mass, and the topology of the intensity profile is utilized incombination with the matching of tandem mass spectra, it is possible to achieve repeat analysis with avery high reproducibility.
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Optimization of a Vacuum Ultraviolet Photoionization source for GC used with a High Resolution TOFMSPoster
-Tune solution allows optimization of ion source parameters for
both proton transfer and direct ionization
-Independent ionization processes exist for M+ and MH+
-Optimizing for dopant signal intensity yields inferior results
-Degree of fragmentation remains relatively constant over a
range of source conditions
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