title: Quantitative affinity purification mass spectrometry: a versatile technology to study protein-protein interactions.
abstract: While the genomic revolution has dramatically accelerated the discovery of disease-associated genes, the functional characterization of the corresponding proteins lags behind. Most proteins fulfill their tasks in complexes with other proteins, and analysis of protein-protein interactions (PPIs) can therefore provide insights into protein function. Several methods can be used to generate large-scale protein interaction networks. However, most of these approaches are not quantitative and therefore cannot reveal how perturbations affect the network. Here, we illustrate how a clever combination of quantitative mass spectrometry with different biochemical methods provides a rich toolkit to study different aspects of PPIs including topology, subunit stoichiometry, and dynamic behavior.
authors.affiliation: Proteome Dynamics, Max Delbrück Center for Molecular Medicine , Berlin, Germany.
authors.forename: Katrina
authors.initials: K
authors.lastname: Meyer
authors.affiliation: Proteome Dynamics, Max Delbrück Center for Molecular Medicine , Berlin, Germany.
authors.forename: Matthias
authors.initials: M
authors.lastname: Selbach
keywords: cross-linking; mass spectrometry based proteomics; protein–protein interaction; quantitative proteomics; stoichiometry