Use of singular value decomposition analysis to differentiate phosphorylated precursors in strong cation exchange fractions.

ABSTRACT: We studied the use of peak deviations (PDs) for application in phosphoproteomics. Due to the differences in the mass defects, the PDs of samples containing mixtures of phosphorylated and nonphosphorylated peptides show bimodal distributions. The ratios of peak heights accurately predict the phosphoproteome content of a sample. In this work, we apply a signal-processing tool, singular value decomposition, to reveal characteristic features of the phosphorylated, nonphosphorylated, and mixed samples. We show that a simple application of singular value decomposition to the PD matrix (i) detects transitions from mostly phosphorylated samples to mostly nonphosphorylated samples, (ii) reveals modes of low-abundance species in the presence of the high-abundance species (e.g., phosphorylated peptid

SUBMITTER: Sadygov RG 

PROVIDER: S-EPMC4518547 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature