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Targeted Mass Spectrometry
Targeted mass spectrometry is a mass spectrometry technique that uses multiple stages of tandem mass spectrometry Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more mass analyzers are coupled together using an additional reaction step to increase their abilities to analyse chemical samples. A com ... (MSn with n=2 or 3) for ions of specific mass ('' m/z''), at specific time. The values of the ''m/z'' and time are defined in an inclusion list which is derived from a previous analysis. Applications Targeted analysis allows the thorough analysis of all ions, at all abundance range above the noise level, at any time window in the experiment. In contrast, non-targeted analysis would, typically, only allow detection of the most abundant 50-100 ions over the entire experiment time. Such limitation of non-targeted analysis makes it less suitable for analyzing highly complex, highly dynamic sample such as human blood serum. ...
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Mass Spectrometry
Mass spectrometry (MS) is an analytical technique that is used to measure the mass-to-charge ratio of ions. The results are presented as a ''mass spectrum'', a plot of intensity as a function of the mass-to-charge ratio. Mass spectrometry is used in many different fields and is applied to pure samples as well as complex mixtures. A mass spectrum is a type of plot of the ion signal as a function of the mass-to-charge ratio. These spectra are used to determine the elemental or isotopic signature of a sample, the masses of particles and of molecules, and to elucidate the chemical identity or structure of molecules and other chemical compounds. In a typical MS procedure, a sample, which may be solid, liquid, or gaseous, is ionized, for example by bombarding it with a beam of electrons. This may cause some of the sample's molecules to break up into positively charged fragments or simply become positively charged without fragmenting. These ions (fragments) are then separated accordin ...
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Tandem Mass Spectrometry
Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more mass analyzers are coupled together using an additional reaction step to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides. The molecules of a given sample are ionized and the first spectrometer (designated MS1) separates these ions by their mass-to-charge ratio (often given as m/z or m/Q). Ions of a particular m/z-ratio coming from MS1 are selected and then made to split into smaller fragment ions, e.g. by collision-induced dissociation, ion-molecule reaction, or photodissociation. These fragments are then introduced into the second mass spectrometer (MS2), which in turn separates the fragments by their m/z-ratio and detects them. The fragmentation step makes it possible to identify and separate ions that have very similar m/z-ratios in regular mass spectrometers. Struc ...
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Data-independent Acquisition
In mass spectrometry, data-independent acquisition (DIA) is a method of molecular structure determination in which all ions within a selected '' m/z'' range are fragmented and analyzed in a second stage of tandem mass spectrometry. Tandem mass spectra are acquired either by fragmenting all ions that enter the mass spectrometer at a given time (called broadband DIA) or by sequentially isolating and fragmenting ranges of '' m/z''. DIA is an alternative to data-dependent acquisition (DDA) where a fixed number of precursor ions are selected and analyzed by tandem mass spectrometry. Broadband One of the first DIA approaches was a nozzle-skimmer dissociation method called shotgun collision-induced dissociation (CID). Fragmentation can be in the ion source of the mass spectrometer by increasing the nozzle-skimmer voltage in electrospray ionization. MSE is a broadband DIA technique that uses alternating low-energy CID and high-energy CID. The low-energy CID is used to acquire precursor ion ...
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