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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.
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
The software evaluates protein sequences from a database to compute the list of peptides that could result from each. The peptide's intact mass is known from the mass spectrum, and Sequest uses this information to determine the set of candidate peptides sequences that could meaningfully be compared to the spectrum by including only those near ...
A peptide spectral library is a curated, annotated and non-redundant collection/database of LC-MS/MS peptide spectra. One essential utility of a peptide spectral library is to serve as consensus templates supporting the identification of peptides and proteins based on the correlation between the templates with experimental spectra.
While the mascots of Democrats and Republicans are well known, you may not be aware of the origins behind them. The Democratic donkey was first used in Andrew Jackson's 1828 presidential campaign.
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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