How does data independent acquisition work?
Data-independent acquisition (DIA) proteomics is a recently-developed global mass spectrometry (MS)-based proteomics strategy.
In a DIA method, precursor ions are isolated into pre-defined isolation windows and fragmented; all fragmented ions in each window are then analyzed by a high-resolution mass spectrometer..
How does swath MS work?
The basic principle is that ions are selected based on the change in the electric fields between quadrupoles.
The first quadrupole Q1 selects ions with a certain mass/charge ratio, and the second quadrupole Q2 acts as the collision chamber to induce fragmentation reaction, and then scans the debris ions in a TOF..
What is data independent analysis in mass spectrometry?
In a DIA analysis, all peptides within a defined mass-to-charge (m/z) window are subjected to fragmentation; the analysis is repeated as the mass spectrometer marches up the full m/z range.
This results in accurate peptide quantification without being limited to profiling predefined peptides of interest..
What is swath analysis in DIA?
SWATH DIA helps generate a permanent digital proteome map with highly reproducible retrospective analysis of cellular and tissue specimens.
It combines quantitative reproducibility with the speed and sensitivity gains of modern mass spectrometers..
What is the swath MS method?
Sequential Window Acquisition of all Theoretical Mass Spectra (SWATH-MS) a specific variant of data-independent acquisition (DIA) method, supports quantitative analysis of peptides up to 9000 of proteins with high quantitative accuracy and consistency..
What is TMT based quantitative proteomics analysis?
TMT quantification belongs to the isobaric isotope labeling quantitative method, and remains the most widely adopted approach among quantitative methods.
The mass-tagging reagent within a set consists of an amine-reactive NHS-ester group (Amine Reactive Group), a spacer arm (balance group), and a mass reporter group..
- Data-independent acquisition (DIA) proteomics is a recently-developed global mass spectrometry (MS)-based proteomics strategy.
In a DIA method, precursor ions are isolated into pre-defined isolation windows and fragmented; all fragmented ions in each window are then analyzed by a high-resolution mass spectrometer. - Quantitative discovery proteomics using mass spectrometry seeks to identify and characterize as many proteins as possible across a broad dynamic range while also measuring the relative protein abundance changes happening in multiple sample sets.
This is also referred to as untargeted proteomics experiments.
