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.
CITATION STYLE
Meyer, K., & Selbach, M. (2015). Quantitative affinity purification mass spectrometry: A versatile technology to study protein-protein interactions. Frontiers in Genetics. Frontiers Media S.A. https://doi.org/10.3389/fgene.2015.00237
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