David Russell

Research Interests

My research focuses on bioanalytical and biophysical chemistry and the development of next-generation native ion mobility and mass spectrometry. Structures and conformational dynamics of proteins, protein complexes and their non-covalent interactions with other molecules are controlled by the Gibbs free energy (GEL) (entropy and enthalpy) of the system. GEL of chemical and biological systems are highly regulated by temperature and solution conditions, but the majority of chemical and biophysical studies are carried out at room, non-physiological temperatures, or even systems lacking temperature control. In order to advance our studies we have developed a novel variable-temperature nano-electrospray ionization (vT-ESI) ion mobility-mass spectrometer with unparalleled sensitivity, dynamic range, and selectivity for studies of both cold- and heat-induced chemical processes. This approach is used for direct determinations of stabilities, reactivities, and thermodynamic measurements on native and non-native proteins and protein complexes as well as protein-ligand interactions. The expansive scope of this approach is the basis for our detection of 40 different conformers of the protein chymotrypsin inhibitor 2, and determination of the thermochemistry for a model membrane protein system binding lipids. The research is funded by NIH and the NIH Resource in Native-MS Guided Structural Biology. Our laboratories in the Interdisciplinary Life Sciences Building (ILSB) and the novel MS instruments provide exciting opportunities for collaborative, interdisciplinary research with chemical-biologists, biochemists and other chemists.