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MALDI TOF/TOF mass spectrometers are used to reveal amino acid sequence of peptides using post-source decay or high energy collision-induced dissociation (further use see mass spectrometry). MALDI-TOF have been used to characterise post-translational modifications. For example, it has been widely applied to study protein methylation and ...
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]
Diagnostic microbiology is the study of microbial identification. Since the discovery of the germ theory of disease , scientists have been finding ways to harvest specific organisms. Using methods such as differential media or genome sequencing , physicians and scientists can observe novel functions in organisms for more effective and accurate ...
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 ...
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]
A time-of-flight mass spectrometer (TOFMS) consists of a mass analyzer and a detector. An ion source (either pulsed or continuous) is used for lab-related TOF experiments, but not needed for TOF analyzers used in space, where the sun or planetary ionospheres provide the ions. The TOF mass analyzer can be a linear flight tube or a reflectron.
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.
Unlike metagenomics, which relies on direct shotgun sequencing or 16S rRNA gene sequencing, culturomics is based on matrix-assisted laser desorption/ionization–time-of-flight (MALDI-TOF) mass spectrometry. [2] However, culturomics also uses 16S RNA sequencing to identify new species. [6] [better source needed]