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MALDI TOF mass spectrometer. In mass spectrometry, matrix-assisted laser desorption/ionization (MALDI) is an ionization technique that uses a laser energy-absorbing matrix to create ions from large molecules with minimal fragmentation. [1]
MALDI mass spectrometry imaging (MALDI-MSI) is the use of matrix-assisted laser desorption ionization as a mass spectrometry imaging [2] technique in which the sample, often a thin tissue section, is moved in two dimensions while the mass spectrum is recorded. [3]
Mascot performs mass spectrometry data analysis through a statistical evaluation of matches between observed and projected peptide fragments. [6] MassMatrix: Freeware: MassMatrix is a database search algorithm for tandem mass spectrometric data. It uses a mass accuracy-sensitive, probabilistic scoring model to rank peptide and protein matches ...
MS 2 – Mass spectrometry/mass spectrometry, i.e. tandem mass spectrometry; MS/MS – Mass spectrometry/mass spectrometry, i.e. tandem mass spectrometry; MALDESI – Matrix-assisted laser desorption electrospray ionization; MALDI – Matrix-assisted laser desorption/ionization; MAII – Matrix-assisted inlet ionization; MAIV – Matrix ...
A Bradbury–Nielsen shutter is a type of ion gate used in TOF mass spectrometers and in ion mobility spectrometers, as well as Hadamard transform TOF mass spectrometers. [9] The Bradbury–Nielsen shutter is ideal for fast timed ion selector (TIS)—a device used for isolating ions over narrow mass range in tandem (TOF/TOF) MALDI mass ...
MALDESI source can also be coupled to drift tube ion mobility spectrometer-mass spectrometer (IMS-MS) for high-throughput screening. [15] These integrations provide more reliable raw data for MSI as well as direct analysis of various biological specimens because long analysis time could cause physiological changes to the samples under ...
In SEAC, the sample surface is modified to bind the analyte of interest for analysis with laser desorption/ionization mass spectrometry (LDI-MS). [ 1 ] [ 4 ] [ 6 ] SEPAR is a combination of SEND and SEAC; the modified sample surface also acts as an energy absorbing matrix for ionization.
Trypsin cleaves the protein after every arginine or lysine amino acid in its sequence, resulting in peptide fragments of predictable masses. After digestion the sample is filtered with C18 filters to get rid of non-proteinaceous material and the sample is now ready for mass spectrometric analysis, which for ZooMS generally means MALDI-TOF MS.