Proteomics Glossary
25 essential terms — because precise language is the foundation of clear thinking in Proteomics.
Showing 25 of 25 terms
A deep learning system for predicting protein three-dimensional structures from amino acid sequences with near-experimental accuracy.
The application of computational methods to analyze biological data, essential for processing and interpreting large-scale proteomics datasets.
A measurable indicator of a biological state or condition, often a protein or peptide identified through proteomic analysis.
A workflow in which proteins are enzymatically digested into peptides prior to MS analysis for protein identification.
An MS strategy that fragments all precursor ions in systematic m/z windows for comprehensive and reproducible analysis.
A soft ionization method producing multiply charged ions from solution-phase analytes, standard for LC-MS proteomics.
The expected proportion of false positives among accepted identifications, typically controlled at 1% using target-decoy approaches.
The attachment of sugar moieties to proteins, affecting folding, stability, and cell-cell recognition.
The complete network of protein-protein interactions within a cell or organism.
Isobaric Tags for Relative and Absolute Quantification, a chemical labeling method for multiplexed proteomics.
A quantitative proteomics strategy estimating protein abundance from peptide ion intensities or spectral counts without isotopic labels.
A separation technique that partitions analytes between a liquid mobile phase and a stationary phase, used to reduce sample complexity before MS.
Matrix-Assisted Laser Desorption/Ionization, a technique generating ions from a crystalline matrix for MS analysis.
An analytical technique that measures the mass-to-charge ratio of ions for molecular identification and quantification.
The addition of a phosphate group to serine, threonine, or tyrosine residues, a key regulatory PTM in cell signaling.
A covalent chemical modification to a protein after its synthesis, regulating its activity, localization, or interactions.
A distinct molecular form of a protein product from a single gene, including variations from splicing, mutations, and PTMs.
The complete set of proteins expressed by a cell, tissue, or organism under defined conditions.
Stable Isotope Labeling by Amino acids in Cell culture, a metabolic labeling method for quantitative proteomics.
A technique involving two stages of mass analysis: precursor ion selection and fragmentation followed by fragment ion detection.
Tandem Mass Tags, isobaric chemical labels enabling multiplexed quantitative comparison of protein abundance.
An approach analyzing intact proteins by MS without prior digestion, preserving proteoform-level information.
A serine protease that cleaves peptide bonds at the C-terminal side of lysine and arginine residues, the standard enzyme for bottom-up proteomics.
A protein separation method using isoelectric focusing and SDS-PAGE to resolve proteins by charge and molecular weight.
The attachment of ubiquitin to a protein, often signaling it for proteasomal degradation.