DIP-MS: ultra-deep interaction proteomics for the deconvolution of protein complexes.

ABSTRACT: Most proteins are organized in macromolecular assemblies, which represent key functional units regulating and catalyzing most cellular processes. Affinity purification of the protein of interest combined with liquid chromatography coupled to tandem mass spectrometry (AP-MS) represents the method of choice to identify interacting proteins. The composition of complex isoforms concurrently present in the AP sample can, however, not be resolved from a single AP-MS experiment but requires computational inference from multiple time- and resource-intensive reciprocal AP-MS experiments. Here we introduce deep interactome profiling by mass spectrometry (DIP-MS), which combines AP with blue-native-PAGE separation, data-independent acquisition with mass spectrometry and deep-learning-based signal pro

SUBMITTER: Frommelt F 

PROVIDER: S-EPMC11009110 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature