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Atmospheric pressure chemical ionization chamber cross section. Atmospheric pressure chemical ionization (APCI) is an ionization method used in mass spectrometry which utilizes gas-phase ion-molecule reactions at atmospheric pressure (10 5 Pa), [1] [2] commonly coupled with high-performance liquid chromatography (HPLC). [3]
The use of the term mass spectroscopy is now discouraged due to the possibility of confusion with light spectroscopy. [1] [8] Mass spectrometry is often abbreviated as mass-spec or simply as MS. [1] Modern techniques of mass spectrometry were devised by Arthur Jeffrey Dempster and F.W. Aston in 1918 and 1919 respectively.
The original interface between capillary zone electrophoresis and mass spectrometry was developed in 1987 [9] by Richard D. Smith and coworkers at Pacific Northwest National Laboratory, and who also later were involved in development of interfaces with other CE variants, including capillary isotachophoresis and capillary isoelectric focusing.
In mass spectrometry, direct analysis in real time (DART) is an ion source that produces electronically or vibronically excited-state species from gases such as helium, argon, or nitrogen that ionize atmospheric molecules or dopant molecules. The ions generated from atmospheric or dopant molecules undergo ion-molecule reactions with the sample ...
Mass spectrometry imaging (MSI) is a technique used in mass spectrometry to visualize the spatial distribution of molecules, as biomarkers, metabolites, peptides or proteins by their molecular masses. After collecting a mass spectrum at one spot, the sample is moved to reach another region, and so on, until the entire sample is scanned.
Fourier-transform ion cyclotron resonance (FTICR) mass spectrometry is a high-resolution technique that can be used to determine masses with high accuracy. Many applications of FTICR-MS use this mass accuracy to help determine the composition of molecules based on accurate mass. This is possible due to the mass defect of the elements.
A major application for ESI is the field of protein mass spectrometry. Here, the MS is used for the identification and sizing of proteins. The identification of a protein sample can be done in an ESI-MS by de novo peptide sequencing (using tandem mass spectrometry) or peptide mass fingerprinting.
Both, the first mass analyzer and the collision cell are continuously exposed to ions from the source, in a time independent manner. [4] It is once the ions move into the third mass analyzer that time dependence becomes a factor. [4] The first quadrupole mass filter, Q1, is the primary m/z selector after the sample leaves the ionization source.