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| Hello everyone, I am interested in quantitative proteomics. Unfortunately I just started learning about these things and I have a lot of doubts and questions (due to the fact that my background is IT more than biological). As far as I understood in order to quantify peptides (after the identification stage) from MS or MS/MS data the "single ion chromatogram" is reconstructed for each identified peptide and the intensities from the chromatogram are used to quantify. Can you please explain me in simple words what the "single ion chromatogram" is and how it can be reconstructed from ms or ms/ms information for some particular peptides? Sorry if my questions are too naive, but I just started. Any help will be appreciated even pointers to the literature where I can learn these things. Thanks in advance. |
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| Hi, found this: Selected ion monitoring (SIM) In the single ion mass chromatogram a small mass window is monitored such that the mass chromatogram represents detection of a very specific mass. Other masses are ignored. This term most often refers to the case where the experiment was designed to achieve this type of data from the beginning. A related term is the extracted ion chromatogram which appears the same however has been reconstructed from a larger data set not exclusively designed to produce a single ion chromatogram. The quality of data from an extracted ion chromatogram is often inferior. Generally, a mass scan is done first in the range of m/z ratios of interest. This allows for identification of the specific m/z that you want to selectively monitor in SIM mode. |