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The original MALDESI design was implemented using common organic matrices, similar to those used in MALDI, along with a UV laser. The current MALDESI source employs endogenous water or a thin layer of exogenously deposited ice as the energy-absorbing matrix where O-H symmetric and asymmetric stretching bonds are resonantly excited by a mid-IR ...
The term matrix-assisted laser desorption ionization (MALDI) was coined in 1985 by Franz Hillenkamp, Michael Karas and their colleagues. [3] These researchers found that the amino acid alanine could be ionized more easily if it was mixed with the amino acid tryptophan and irradiated with a pulsed 266 nm laser.
A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]
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Target for MALDI imaging with two conductive-surface microscope slides. Sample preparation is a critical step in imaging spectroscopy. Scientists take thin tissue slices mounted on conductive microscope slides and apply a suitable MALDI matrix to the tissue, either manually or automatically.
A reflectron (mass reflectron) is a type of time-of-flight mass spectrometer (TOF MS) that comprises a pulsed ion source, field-free region, ion mirror, and ion detector and uses a static or time dependent electric field in the ion mirror to reverse the direction of travel of the ions entering it.
It is a variation of matrix-assisted laser desorption/ionization (MALDI). [ 1 ] [ 2 ] In MALDI, the sample is mixed with a matrix material and applied to a metal plate before irradiation by a laser, [ 3 ] whereas in SELDI, proteins of interest in a sample become bound to a surface before MS analysis.