Native mass spectrometry is a powerful tool for the structural biology studies of macromolecular assemblies.  The top-down MS of proteins and noncovalent protein complexes in near physiological solution conditions provides information on binding sites, stoichiometry, and exposed surface of proteins or complexes.

Recent Publications

Wongkongkathep P, Han JY, Choi TS, Yin S, Kim HI, Loo JA. 2018. Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein. J. Am. Soc. Mass Spectrom. 29(9):1870–80
Zhang Y, Cui W, Wecksler AT, Zhang H, Molina P, et al. 2016. Native MS and ECD Characterization of a Fab–Antigen Complex May Facilitate Crystallization for X-ray Diffraction. J. Am. Soc. Mass Spectrom. 27(7):1139–42
Savaryn JP, Skinner OS, Fornelli L, Fellers RT, Compton PD, et al. 2016. Targeted analysis of recombinant NF kappa B (RelA/p65) by denaturing and native top down mass spectrometry. Journal of Proteomics. 134:76–84
Zhang J, Malmirchegini GR, Clubb RT, Loo JA. 2015. Native Top-down Mass Spectrometry for the Structural Characterization of Human Hemoglobin. Eur J Mass Spectrom (Chichester). 21(3):221–31
Li H, Wongkongkathep P, Orden SLV, Loo RRO, Loo JA. 2014. Revealing Ligand Binding Sites and Quantifying Subunit Variants of Noncovalent Protein Complexes in a Single Native Top-Down FTICR MS Experiment. J. Am. Soc. Mass Spectrom. 25(12):2060–68
Marty MT, Zhang H, Cui W, Blankenship RE, Gross ML, Sligar SG. 2012. Native Mass Spectrometry Characterization of Intact Nanodisc Lipoprotein Complexes. Anal. Chem. 84(21):8957–60
Yin S, Loo JA. 2011. Top-down mass spectrometry of supercharged native protein–ligand complexes. International Journal of Mass Spectrometry. 300(2):118–22