Hands on Native Mass Spectrometry Analysis of Multi-protein Complexes

Stéphane Erb (1) , Sarah Cianférani (1) , Julien Marcoux (2)

1 DSA-IPHC - Département Sciences Analytiques et Interactions Ioniques et Biomoléculaires
2 IPBS - Institut de pharmacologie et de biologie structurale

By maintaining intact multi-protein complexes in the gas-phase, native mass spectrometry provides their molecular weight with very good accuracy compared to other methods (typically native PAGE or SEC-MALS) [1]. Besides, heterogeneous samples, both in terms of oligomeric states and ligand-bound species can be fully characterized. Here we thoroughly describe the analysis of several oligomeric protein complexes ranging from a 16 kDa dimer to a 801 kDa tetradecameric complex on different instrumental setups.

Mots clés: Structural Mass Spectrometry; Non Covalent Mass Spectrometry; Oligomeric states; Stoichiometry; Subcomplexes

Domaines: Chimie

Stéphane Erb, Sarah Cianférani, Julien Marcoux. Hands on Native Mass Spectrometry Analysis of Multi-protein Complexes. Arnaud Poterszman. Multiprotein Complexes : Methods and Protocols, 2247, Spinger; Humana, pp.173-191, 2021, Methods in Molecular Biology, 978-1-0716-1125-8. ⟨10.1007/978-1-0716-1126-5_10⟩. ⟨hal-03056883⟩