My research focuses on proteomics, lipidomics, biophysical chemistry and application and development of mass spectrometry, such as \"label-free\" nano-particle based biosensors and novel peptide/protein isolation and purification strategies. We are also investigating the structure(s) of model peptides in an effort to better describe folding/unfolding and structure of membrane and intrinsically disordered (IDP) proteins. Peptides take on very different 2?, 3? and 4? structure, which determine or influence bio-activity. In the presence of lipid vesicles peptides can exist as solution-phase species, \"absorbed\" on lipid bilayers or \"inserted\" (as a monomer or multimer) in lipid bilayers. By what mechanism do peptides interact with lipid membranes to affect these structural changes, how do peptide-lipid interactions promote self-assembly to form intermediates that eventually yield aggregates, i.e., amyloid fibrils, or how does metal ion coordination affect the structure of metalloproteins? Mass spectrometry-based experiments, hydrogen/deuterium (H/D) exchange, chemical 'foot-printing' and gas-phase (ion-molecule and ion-ion reaction chemistry) and solution-phase chemical modifications, have expanded our abilities to address such questions, and new instrumental approaches, esp. ion mobility spectrometry (IMS) combined with enhanced molecular dynamics simulations (MDS), have become standard tools for structural-mass spectrometry studies. Over the past several years we have either acquired or developed novel, next-generation IM-MS instruments that are redefining cutting-edge structural-mass spectrometry research as well as cutting-edge computational tools essential to carry out these studies. Our new laboratories in the Interdisciplinary Life Sciences Building (ILSB) provides exciting opportunities for collaborative, interdisciplinary research with chemical-biologists, biochemists and other chemists.
Academic Articles581
- Zheng, X., Kurulugama, R. T., Laganowsky, A., & Russell, D. H. (2020). Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer.. Analytical® Chemistry.
- Lin, C., McCabe, J. W., Russell, D. H., & Barondeau, D. P. (2020). Molecular Mechanism of ISC Iron-Sulfur Cluster Biogenesis Revealed by High-Resolution Native Mass Spectrometry.. Journal of the American Chemical Society. 142(13), 6018-6029.
- Shirzadeh, M., Poltash, M. L., Laganowsky, A., & Russell, D. H. (2020). Structural Analysis of the Effect of a Dual-FLAG Tag on Transthyretin. BIOCHEMISTRY. 59(9), 1013-1022.
- Hebert, M. J., & Russell, D. H. (2020). Tracking the Structural Evolution of 4-Aminobenzoic Acid in the Transition from Solution to the Gas Phase.. The journal of physical chemistry. B. 124(11), 2081-2087.
- Dong, S., Shirzadeh, M., Fan, L., Laganowsky, A., & Russell, D. H. (2020). Ag+ Ion Binding to Human Metallothionein-2A Is Cooperative and Domain Specific.. Analytical® Chemistry. 92(13), 8923-8932.
Conference Papers155
- Liu, Y., Liu, W., Poltash, M., Russell, D., & Laganowsky, A. (2019). Native ion mobility mass spectrometry of membrane protein complexes. ACS Photonics. 257,
- Russell, D. (2018). Native-ESI and ion mobility-mass spectrometry: Expanding MS-based structural biology through understanding of chemical fundamentals. ACS Photonics. 255,
- Russell, D. (2017). Mapping peptide/protein conformation space: A challenge for IM-MS. ACS Photonics. 253,
- Rogers, D., El-Baba, T., Shi, L., Khan, F., Kim, D., Hales, D., Russell, D., & Clemmer, D. (2016). Histidine-modified polyproline-13 explores the nature of two-state cooperativity. ACS Photonics. 251,
Patents5
- Mclean, J., Russell, D., Egan, T., Ugarov, M., & Schultz, A. (2010). Multiplex data acquisition modes for ion mobility-mass spectrometry.
- Mclean, J., Russell, D., Egan, T., Ugarov, M., & Schultz J. A., .. (2008). Multiplex data acquisition modes for ion mobility-mass spectrometry.
- Russell, D., & Mclean, J. (2007). Advanced optics for rapidly patterned laser profiles in analytical spectrometry.
- Mclean, J., Russell, D., & Schultz, A. (2006). Gas-phase purification of biomolecules by ion mobility for patterning microarrays and protein crystal growth.
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- CHEM315 Fund. Of Quant. Analysis Instructor
- CHEM415 Analytical Chemistry Instructor
- CHEM491 Research Instructor
- CHEM681 Seminar Instructor
- CHEM689 Sptp:biological Mass Spectr Instructor
- Kim, Doyong (2016-08). Monitorying the Desolvaiton of Ions and Create Candidate Structure for the Ions Detected by Ion Mobility-Mass Spectrometry Study by Molecular Dynamics Simulations. (Doctoral Dissertation)
- Servage, Kelly Anne (2016-08). Investigating the Effects of Dehydration on the Conformational Preferences of Biomolecules during the Final Stages of Electrospray Ionization. (Doctoral Dissertation)
- Lang, Phillip (2016-05). An Investigation of Polymer Encapsualted Gold Nanoparticles for Use in Analytical Methods for Proteomic Based Research. (Master's Thesis)
- Xiao, Chunying (2015-12). Effects of Charge States, Charge Sites and Side Chain Interactions on Conformational Preferences of a Series of Model Peptide Ions. (Master's Thesis)