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Mascot identifies proteins by interpreting mass spectrometry data. The prevailing experimental method for protein identification is a bottom-up approach, where a protein sample is typically digested with trypsin to form smaller peptides. While most proteins are too large, peptides usually fall within the limited mass range that a typical mass ...
The MOWSE algorithm was developed by Darryl Pappin at the Imperial Cancer Research Fund and Alan Bleasby at the SERC Daresbury Laboratory. [2] The probability-based MOWSE score formed the basis of development of Mascot, a proprietary software for protein identification from mass spectrometry data.
The mass spectrum serves as a fingerprint in the sense that it is a pattern that can serve to identify the protein. [1] The method for forming a peptide-mass fingerprint, developed in 1993, consists of isolating a protein, breaking it down into individual peptides, and determining the masses of the peptides through some form of mass ...
SEQUEST is a MS data analysis program used for protein identification. It correlates collections of tandem mass spectra to peptide sequences that have been generated from databases of protein sequences. [21] SIMS Open source: SIMS was designed to perform unrestricted PTM searches over tandem mass spectra. [22] SimTandem Freeware
These methods determined the mass of peptides using mass spectrometry, and then used the mass to search protein databases to identify the proteins [3] [4] In 1999 a more complex program was released called Mascot that integrated three types of protein/database searches: peptide molecular weights, tandem mass spectrometry from one or more ...
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]
Such derivative patterns are used as templates to find a sufficiently close match within experimental mass spectra, which serves as the basis for peptide/protein identification. Many tools have been developed for this practice, which have enabled many past discoveries, e.g. SEQUEST, [3] Mascot. [4]
This further challenges the identification of the peptide sequence by means of conventional database matching approaches. Together with peptide fragmentation spectra of poor quality or high complexity (due to co-isolation or sensitivity limitations), this leaves in a conventional shotgun proteomics experiment many sequencing spectra unidentified.