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Protein Identification by MALDI-MS Peptide Mass Mapping

Protein Identification by MALDi-MS Peptide Mass Mapping [Pg.119]

The introduction of delayed ion extraction in MALDI-TOF instruments in 1995 resulted in a tremendous improvement in analytical performance, mass resolution and accuracy. Using this technique, peptide mass mapping gained high specificity for protein identification and an ability to identify individual components among simple protein mixtures [60, 61]. Improved sample preparation methods also provided an enhanced sensitivity to enable analysis of femtomolar levels of protein [5, 19], Today, the automation of MALDI-MS data acquisition enables the analysis of hundreds of samples each day in large-scale protein identification experiments [62]. [Pg.120]

Protein score is -IQ Loi CP), where P is the probability that the observed matdi is a random event Protein scores greater than 76 are significant (p 0.05). [Pg.121]

BAB22149 AK002501 NID Mass 30109 Score 151 - Mus nusculus Expect 1. 9e-09 Queries matched 9 [Pg.121]

End Observed Ur(e)q t) Hr eale) Delta Ulss Sequence [Pg.121]


Figure 3.9 Principle of protein identification by MALDI-MS peptide mass mapping. The experimentally determined MALDI-MS peptide mass map is compared to protein... Figure 3.9 Principle of protein identification by MALDI-MS peptide mass mapping. The experimentally determined MALDI-MS peptide mass map is compared to protein...

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