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Rational Numbers Excel Add-In Proprietary: De novo identification tool for small molecules that works with Microsoft Excel (2010, 2013, 2016 and 2019). This software treats small molecules as mathematical partitions of the molecular mass and generates subfragment formulas with atoms that are sets of partitions comprising the molecular formula.
BASys (Bacterial Annotation System) is a tool for automated annotation of bacterial genomic (chromosomal and plasmid) sequences including gene/protein names, GO functions, COG functions, possible paralogues and orthologues, molecular weights, isoelectric points, operon structures, subcellular localization, signal peptides, transmembrane regions ...
Peptide amphiphiles were developed in the 1990s. They were first described by the group of Matthew Tirrell in 1995. [5] [6] These first reported PA molecules were composed of two domains: one of lipophilic character and another of hydrophilic properties, which allowed self-assembly into sphere-like supramolecular structures as a result of the association of the lipophilic domains away from the ...
The program cleaves every protein in the specified search database in silico according to specific rules depending on the cleavage enzyme used for digestion and calculates the theoretical mass for each peptide. Mascot then computes a score based on the probability that the peptides from a sample match those in the selected protein database.
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. [citation ...
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
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]
Peptide fragmentation notation using the scheme of Roepstorff and Fohlman (1984). [5] A notation has been developed for indicating peptide fragments that arise from a tandem mass spectrum. [5] Peptide fragment ions are indicated by a, b, or c if the charge is retained on the N-terminus and by x, y or z if the charge is maintained on the C ...