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FHCRC MALDI Dilution Processed Data

Dataset Abstract:

These data come from a dilution experiment aimed at elucidating which features in MALDI-TOF mass spectrometry data are informative for quantifying peptide content. The details of the experiment are described in [1]. The primary dataset consists of 250 spectra collected from 5 different serum sources (5 people from a health study), each subject to 10 different concentrations of a peptide mixture that contained several known peptides. Each of the 50 prepared samples were spotted, randomly, 5 times each on a single plate producing a total of 5x10x5 = 250 spectra. An additional 30 spectra arise from: 2 replicate spectra from each of the 10 concentrations of the peptide mixture, plus 2 replicates of serum-only spectra from each of the 5 serum samples. NOTE: An error was made during the process of randomly spotting samples to the plate: one of the replicates from concentration 6 was spotted on top of a serum-only sample. The result is that two spectra from this design are missing: serum 1, concentration 6, replicate 4 (column number 36 in Spectra.txt), and serum 4, concentration 0, replicate 2. This left one empty spot on the plate (column number 280 in Spectra.txt) to which we spotted a sample containing only cytochrome c. The latter was not used in any subsequent analysis in [1], and no adjustment was made for former in the analysis in [1] (column #36 was used as is).

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FHCRC MALDI Dilution Processed Data
Timothy W. Randolph
Dale McLerran
Prostate and Urologic
Under Review
This work addresses the problem of extracting signal content from protein mass spectrometry data. A multiscale decomposition of these spectra is used to focus on local scale-based structure by defining scale-specific features. Quantification of features is accompanied by an efficient method for calculating the location of features which avoids estimation of signal-to-noise ratios or bandwidths.
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