Mass Spectrometry (MS) based Proteomics Sample Clauses

Mass Spectrometry (MS) based Proteomics. In proteomics, before analyzing the expression levels of proteins in a given sample, the protein complement of that sample needs to be accurately and efficiently identified. This is afforded by a suite of technological tools broadly called mass spectrometry. Mass spectrometry is a powerful technique that is used to identify unknown com- pounds, to quantify known compounds, and to elucidate the structure and chem- ical properties of molecules. The introduction of two ionization techniques in the mid-1980s: ESI (ElectroSpray Ionization) and MALDI (Matrix Assisted Laser Des- orption/Ionization), transformed MS into an enabling technology in proteomics by allowing ionization of large intact macromolecules such as peptides and proteins. Mass spectrometry based proteomics has emerged as the preferred and most power- ful technological approach in proteomics studies. many improvements over the last decade in both instrumentation and associated computing tools now allow the rapid processing of high-throughput data, leading to accurate and routine protein identi- fication, quantification, and determination of sites of post-translational modification (Aebersold et al., (2003)) [1]. In proteomics, the typical output from a mass spectrometer are spectra that com- prise of digitized arrays of the intensities of all discrete mass-to-charge ratios detected over a discrete mass range. A specialized MS procedure known as tandem mass spec- trometry (MS/MS) is widely used to sequence peptides in real-time during the MS operation. Interpretable MS/MS spectra are usually produced after only about 1-2 seconds of data acquisition time, and the entire process of pre-cursor peptide selec- tion and MS/MS analysis can be fully automated. This allows the high-throughput, large-scale analysis of complex protein mixtures in a fairly rapid and sensitive manner. The MS method of first ionizing intact proteins using either ESI or MALDI, and then introducing them to a mass analyzer, is referred to as the ”top-down” strategy of protein analysis. Conversely, the ”bottom-up” strategy first digests protein analytes into smaller peptides, enzymatically or by chemical cleaving, before being fed into the mass spectrometer.
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Related to Mass Spectrometry (MS) based Proteomics

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