Mass spectrometry has potential as a tool for ecological studies and bioprospecting of natural products from marine cyanobacteria and algae.

Comprehensive structural and compositional characterization of the in vivo 30S ribosomal assembly landscape reveals parallel pathways for 3′-domain formation and a previously unknown role for the assembly factor RimP.

As the function of membrane proteins is often influenced by its membrane environment the presented combinatorial approach is of great value for the investigation of membrane protein complexes in natural or even manipulated lipid bilayers.

By performing ¹⁵N pulse-labeling of mice, the turnover of hundreds of proteins in eye tissues was measured by mass spectrometry that revealed long-lived metabolic enzymes in the lens.

Comprehensive mass spectrometry analysis of human plasma proteome reveals tissue leakage proteins, describes variability between individual plasma proteomes and demonstrates protein transfer across the placenta during pregnancy.

Hydrogen-deuterium exchange mass spectrometry reveals nucleotide-driven conformational regulation of Sec protein-channel to help impose directionality for protein transport through the Sec complex.

A community-based international effort generates standardized HLA allele-specific peptide assay libraries and enables the analysis of the human immunopeptidome by SWATH mass spectrometry.

Molecular details of how the iron–sulfur cluster cofactor of a bacterial global iron regulatory protein simultaneously senses iron and O₂ are revealed by mass spectrometry and spectroscopy.

Mass spectrometry on plasma from patients with typhoid fever and other febrile disease identified and validated 24 metabolites that can distinguish typhoid from other febrile diseases, providing a new approach for typhoid diagnostics.

An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.