Hands on Native Mass Spectrometry Analysis of Multi-protein Complexes.

Methods in molecular biology (Clifton, N.J.) (2020-12-11)
Stéphane Erb, Sarah Cianférani, Julien Marcoux

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) (Marcoux and Robinson, Structure 21:1541-1550, 2013). Besides, heterogeneous samples, in terms of both 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.

Product Number
Product Description

Chaperonin 60 from Escherichia coli, >95% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder
Concanavalin A from Canavalia ensiformis (Jack bean), Type IV-S, lyophilized powder, aseptically processed, BioReagent, suitable for cell culture