文摘
As proteomics continues to establish itself as an effectivepostgenomic research tool, there is an increasingly urgentneed for efficient, automated analysis techniques capableof effectively dealing with the vast amounts of data generated via mass spectrometry. Wholesale analysis packages,often used to deal with these enormous amounts of data,may benefit from supplementary, targeted analyses ascurrent research begins to emphasize posttranscriptional/translational protein modifications, protein truncations,and poorly characterized mutations. We demonstrate theapplication of a new analysis technique based on mathematical correlation that is computationally efficient androbust against different instruments, noise levels, andexperimental conditions. We have previously shown thatthis technique is able to extract pertinent mass shiftsignals from MS data, corresponding to the neutral lossof a modification from a peptide, e.g., a loss of 79.97 Thfrom phosphorylated tyrosine. Here we show that anextension of this method is applicable to MS and MS/MSdata in general, allowing visualization of ions that producea particular mass shift signal, be it from differential stableisotope labeling, overlap of fragment ions in a series, orions that produce a neutral loss. The application of thismethod allows the researcher to discover individualfeatures, such as the presence of specific modified orisotopically labeled peptides, to eliminate overlappingfragment ion series, and to localize specific sites ofmodification.