This protocol describes a strategy for cell-specific labeling of nascent proteomes in vivo. Cell-type-specific proteins are tagged with a noncanonical amino acid in live mice and then are subjected to affinity purification and identification by MS.

This protocol describes a single-pot, solid-phase-enhanced sample-preparation (SP3) method for rapid, robust, and efficient processing of protein samples for proteomic analysis.

A proximity-based labeling system, PUP-IT, identifies membrane protein interactions.

Understanding the functions of protein glycosylation critically depends on methods to efficiently enrich glycoproteins from complex samples. Here, the authors develop a strategy using dendrimer-conjugated benzoboroxole to enhance glycopeptide enrichment, providing the basis for more comprehensive glycoprotein analyses.

A twist on a common method used for enriching phosphorylated peptides for mass spectrometry-based proteomics analysis now reveals previously undetected and widespread histidine phosphorylation in Escherichia coli.