Welcome to Dr. David H. Russell's Research Group at the Texas A&M University. Research activities in the Russell Research Group (RRG) 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 different conformers of proteins and determination of the thermochemistry for a model membrane protein system binding lipids. Current research is funded by NIH (R01 and RM1) and The Welch Foundation. 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. Novel instrumentation plays an increasingly important role in biological mass spectrometry and the RRG is actively pursuing new instrument methods centered around ion mobility instruments, and focuses on developing more versatile and sensitive methods for structural characterization.