Department of Chemistry
A headshot

David Russell
Applied Biosystems/MDS Sciex, Instruments Professorship in Mass Spectrometry in Chemistry

Other Affiliations

Department of Chemistry
Texas A&M University
College Station, TX 77843-3255

P: 979-845-3345
F: 979-845-9485

Researcher ID

Current Activities

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.

Educational Background

B. S., 1974, University of Arkansas-Little Rock

Ph. D., 1978, University of Nebraska-Lincoln

Awards & Recognition

  • 2013 Associate Editor, Journal of The American Society for Mass Spectrometry (Critical Insights)
  • 2013 Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry (ACS national award; sponsored by the Waters Corp.)
  • 2006 Fred M. Garland Memorial Lecture and Award
  • 2004 Association of Former Students Distinguished Achievement Award for Research, Texas A&M University
  • 2004 Fellow, American Association for Advancement of Science
  • 2002 AB/MDS Sciex Professor of Mass Spectrometry
  • 1998 NSF Special Creativity Extension Award
  • 1994 Director, Laboratory of Biological Mass Spectrometry

Selected Publications

  • Clemmer, D. E.; Russell, D. H.; Williams, E. R. Characterizing the Conformationome: Toward a Structural Understanding of the Proteome. Accounts Chem. Res. 2017, 50(3), 556–560.
  • Servage, K. A.; Silveira, J. A.; Fort, K. L.; Russell, D. H. Cryogenic Ion Mobility-Mass Spectrometry: Tracking Ion Structure from Solution to the Gas Phase. Accounts Chem. Res. 2016, 49(7), 1421-1428.
  • Cong, X.; Liu, Y.; Liu, W.; Liang, X.; Russell, D. H.; Laganowsky, A. Determining Membrane Protein-Lipid Binding Thermodynamics Using Native Mass Spectrometry. J. Am. Chem. Soc. 2016, 138, 4346-4349.
  • Wagner, N. D.; Kim, D.; Russell, D. H. Increasing Ubiquitin Ion Resistance to Unfolding in the Gas Phase Using Chloride Adduction: Preserving More "Native-Like" Conformations Despite Collisional Activation. Anal. Chem. 2016, 88, 5934-5940.
  • Servage, K. A.; Fort, K. L.; Silveira, J. A.; Shi, L; Clemmer D.E.; Russell, D. H. Unfolding of Hydrated Alkyl Diammonium Cations Revealed by Cryogenic Ion Mobility-Mass Spectrometry. J. Am. Chem. Soc. 2015, 137, 8916-8919.