Native MS Guided Structural Biology Center

Structure of a RecT/Redβ Family Recombinase in Complex with a Duplex Intermediate of DNA Annealing.

Caldwell, B. J.; Norris, A. S.; Karbowski, C. F.; Wiegand, A. M.; Wysocki, V. H.; Bell, C. E.

Nat Commun 2022, 13 (1), 7855. https://doi.org/10.1038/s41467-022-35572-z.

Protein Complex Prediction Using Rosetta, AlphaFold, and Mass Spectrometry Covalent Labeling.

Drake, Z. C.; Seffernick, J. T.; Lindert, S.

Nat Commun 2022, 13 (1), 7846. https://doi.org/10.1038/s41467-022-35593-8.

Performance evaluation of in-source ion activation hardware for collision-induced unfolding of proteins and protein complexes on a drift tube ion mobility-mass spectrometer.

Gadkari, V. V.; Juliano, B. R.; Mallis, C. S.; May, J. C.; Kurulugama, R. T.; Fjeldsted, J.C.; McLean, J. A.; Russell, D. H.; Ruotolo, B. T.

ChemRxiv (2022), 1-13 | 10.26434/chemrxiv-2022-njhrw

Characterization of lipid carbon–carbon double-bond isomerism via ion mobility-mass spectrometry (IMS-MS) combined with cuprous ion-induced fragmentation

Kuo, S.-T.; Tang, S.; Russell, D. H. Yan, X.

International Journal of Mass Spectrometry 2022, 479, 116889. https://doi.org/10.1016/j.ijms.2022.116889.

A novel Y-shaped, S-O-N-O-S-bridged crosslink between three residues C22, C44, and K61 is a redox switch of the SARS-CoV-2 main protease.

Yang, K. S.; Kuo, Sy.-T. Alex; Blankenship, L. R.; Sheng, Y. J.; Sankaran, B.; Li, Pingwei; Fierke, C. A.; Russell, D. H.; Yan, X.; Xu, S.; Liu, W. R.

bioRxiv (2022), 1-20. doi: https://doi.org/10.1101/2022.04.29.490044.

Mechanistic Insights of IscU Conformation Regulation for Fe–S Cluster Biogenesis Revealed by Variable-Temperature Electrospray Ionization Native Ion Mobility Mass Spectrometry.

Lin, C.-W.; Oney-Hawthorne, S. D.; Kuo, S.-T.; Barondeau, D. P.; Russell, D. H.

Biochemistry 2022, 61, 23, 2733–2741. https://doi.org/10.1021/acs.biochem.2c00429

De Novo Design of Obligate ABC-Type Heterotrimeric Proteins.

Bermeo, S.; Favor, A.; Chang, Y.-T.; Norris, A.; Boyken, S. E.; Hsia, Y.; Haddox, H. K.; Xu, C.; Brunette, T. J.; Wysocki, V. H.; Bhabha, G.; Ekiert, D. C.; Baker, D.

Nat Struct Mol Biol 2022, 29 (12), 1266–1276. https://doi.org/10.1038/s41594-022-00879-4.

Cupric Ions Selectively Modulate TRAAK–Phosphatidylserine Interactions.

Zhu, Y.; Schrecke, S.; Tang, S.; Odenkirk, M. T.; Walker, T.; Stover, L.; Lyu, J.; Zhang, T.; Russell, D.; Baker, E. S.; Yan, X.; Laganowsky, A.

J. Am. Chem. Soc. 2022, 144 (16), 7048–7053. https://doi.org/10.1021/jacs.2c00612.

Intrinsically Disordered Interaction Network in an RNA Chaperone Revealed by Native Mass Spectrometry.

Sarni, S. H.; Roca, J.; Du, C.; Jia, M.; Li, H.; Damjanovic, A.; Małecka, E. M.; Wysocki, V. H.; Woodson, S. A.

Proceedings of the National Academy of Sciences 2022, 119 (47), e2208780119. https://doi.org/10.1073/pnas.2208780119.

Thermodynamic Coupling between Neighboring Binding Sites in Homo-Oligomeric Ligand Sensing Proteins from Mass Resolved Ligand-Dependent Population Distributions.

Li, W.; Norris, A. S.; Lichtenthal, K.; Kelly, S.; Ihms, E. C.; Gollnick, P.; Wysocki, V. H.; Foster, M. P.

Protein Sci 2022, 31 (10), e4424. https://doi.org/10.1002/pro.4424.

Native MS Guided Structural Biology Center

Georgia Institute of Technology