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.
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4238047
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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
Lermyte F, Sobott F. 2015. Electron transfer dissociation provides higher-order structural information of native and partially unfolded protein complexes. Proteomics. 15(16):2813–22
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
Li H, Wolff JJ, Van Orden SL, Loo JA. 2014. Native Top-Down Electrospray Ionization-Mass Spectrometry of 158 kDa Protein Complex by High-Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. Anal. Chem. 86(1):317–20
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