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.
May, J.C.; Russell, D.H. A Mass-Selective Variable-Temperature Drift Tube Ion Mobility-Mass Spectrometer for Temperature Dependent Ion Mobility Studies. J. Am. Soc. Mass Spectrom. 2011, 22, 1134-1145.
Pai, P-J.; Cologna, S. M.; Russell, W.K.; Vigh, G.; Russell, D.H. An Efficient Electrophoretic Method to Remove Neutral Additives from Protein Solutions Followed by Mass Spectrometry Analysis. Anal. Chem. 2011, 83, 2814-2818.
Castellana, E.; Gamez, R.; Russell, D.H.; Label-Free Biosensing with Gold Nanorod Supported Lipid Bilayers. J. Am. Chem. Soc. 2011, 133, 4182-4185.
Chen, L.; Shao, Q.; Gao;Y-Q; Russell, D.H. A Molecular Dynamics and Ion Mobility Spectrometry Study of Model β-hairpin Peptide Ions. J. Phys. Chem. B. 2011, 115, 4427-4435.
McLean, J.R.; McLean, J.A.; Wu, Z.; Becker, C.; Perez, L.M.; Pace, C. N.; Scholtz, J.M.; Russell, D.H. Factors that Influence Helical Preference for Singly- Charged Gas-Phase Peptide Ions: The Effects of Multiple Charge-Carrying Sites. J. Phys. Chem. B. 2010, 114, 809-816.