Mass spectrometry (MS)-based strategies have emerged as key elements for structural modelling of proteins and their assemblies.
Not to be IgG‐nored - An integrative strategy combining ion mobility mass spectrometry (IM‐MS) with molecular modelling can be used to study the conformational dynamics of human IgG antibodies. Predictive models of all four human IgG subclasses were assembled and their dynamics sampled in the transition from extended to collapsed state during IM‐MS. The structural representation is in good agreement with the observed collision cross sections.
Mass spectrometry (MS) has emerged as an important tool for the investigation of structure and dynamics of macromolecular assemblies. Here, we integrate MS-based approaches to interrogate protein complex formation and ligand binding.
By combining hybrid mass spectrometry with cryo-EM, computational and biochemical data, we investigate the oligomeric formation of HerA and detail the mechanism of nucleotide binding to the HerA–NurA complex from thermophilic archaea.