Resolving the Complexity of Proteomic Samples with Ion Mobility-Mass Spectrometry

With an increasing demand for laboratory systems to provide meaningful results, the quality and consistency of the information is of paramount importance. In complex proteomic samples MS systems just separating by m/z are running into issues of chimericy and isobaric species. Advances can only come from using an orthogonal dimension of separation, and one that would ideally add no additional instrument time; just better results.

The challenge in current proteomics research is to reliably identify and accurately quantify thousands of proteins over a wide dynamic range. The faster sampling of chromatographic peaks in a serial, data-dependent manner leads to irreproducibility and biases the analysis towards the most abundant peptides. Data-independent analysis (LC-MS^E) yields reproducible fragmentation and peak area information for all detectable peptides. The use of ion mobility during this analysis (LC-HDMS^E) inserts an orthogonal separation in the gas phase, in the millisecond timescale, poised between the chromatographic and mass spectral dimensions. We will talk about improving both sensitivity and specificity in the analysis of a variety of proteomic samples.

This webinar introduces you to HDMS^E and shows its benefits applied to real biological samples.

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