to measure the quantity of something precisely

the total number of spectra identified for a protein during label-free mass spectrometry, measuring protein abundance

a method used to link peaks in mass spectrometry spectra to liquid chromatography, normally by using spike samples to determine absolute quantities

method of attaching a label molecule to lysine residues, allowing mass differences between different H and C isotopes to be identified

method attaching affinity tags to cysteine residues, allowing mass differences from different H isotopes to be identified by mass spectrometry

chemical labels allowing multiplexing of samples in mass spectrometry, and especially useful in the identification of proteins, peptides, and nucleic acids; a type of isobaric mass tags

an isobaric labelling technique used by tandem mass spectrometry (MS/MS), determining the amount of proteins from different sources, in the same experiment; isotope-labelled molecules are covalently bonded to the N-terminus and side chain N-terminus

mass spectrometry technique detecting differences in protein abundance by labelling with non-radioactive isotopes; cells are split into 2 groups, with 1 fed normal amino acids and 1 fed with heavy-isotope labelled amino acids

mass spectrometry technique involving labelling chemical groups with the same mass with heavy isotopes in their chemical structure (also called tandem mass tags)

mass spectrometry analysis technique using two mass spec reactions with a processing step between to fragment particles

method identifying a bait protein to precipitate a protein of interest

method determining physical interactions between 2+ proteins, confirming the interaction between two proteins

method tagging a protein of interest with a known epitope, allowing the fusion protein to be identified with an antibody specific for that tag

a library of antibodies/aptamers/affibodies are arrayed on a chip, capturing complementary molecules as a protein solution (cell lysate, …) is washed over the chip, allowing binding interactions to be analysed

an oligomer of synthetic nucleic acids or peptide, binding a specific target molecule; ‘chemical antibodies’

small, robust protein molecules able to bind a large number of target proteins or peptides with high affinity; antibody mimetic

a large number of purified proteins are immobilised on a chip, allowing protein-protein, protein-DNA, protein-RNA, protein-phospholipid, and protein-small-molecule interactions to be identified; arrayed proteins must retain their native structure

method allowing protein expression levels to be identified from a large number of biological samples simultaneously, where high-quality antibodies are used; samples are immobilised on the chip, and labelled antibody then washed over, with fluorescence or other data obtained

a way of showing interactions between proteins, domains, and peptides, and the affinity of the interactions