Native mass spectrometry (MS) involves the analysis and characterization of
macromolecules, predominantly intact proteins and protein complexes, whereby as much as …

Native mass spectrometry (MS) is aimed at preserving and determining the native structure,
composition, and stoichiometry of biomolecules and their complexes from solution after they …

Native mass spectrometry (MS) has become widely accepted in structural biology, providing
information on stoichiometry, interactions, homogeneity, and shape of protein complexes …

The emergence of SARS-CoV-2 variants threatens current vaccines and therapeutic
antibodies and urgently demands powerful new therapeutics that can resist viral escape. We …

The design of new therapeutic molecules can be significantly informed by studying protein-
ligand interactions using biophysical approaches directly after purification of the protein …

Native mass spectrometry (nMS) is a biophysical method for studying protein complexes and
can provide insights into subunit stoichiometry and composition, protein–ligand, and protein …

Abstract Structure determination of membrane proteins has highlighted the many roles
played by lipids in influencing overall protein architecture. It is now widely accepted that …

Human shelterin is a six-subunit complex—composed of TRF1, TRF2, Rap1, TIN2, TPP1,
and POT1—that binds telomeres, protects them from the DNA-damage response, and …

Combining diverse experimental structural and interactomic methods allows for the
construction of comprehensible molecular encyclopedias of biological systems. Typically …

An increasing number of studies on biomolecular function indirectly combine mass
spectrometry (MS) with imaging techniques such as cryo electron microscopy (cryo-EM) …