Our research defines the relationship between structure, dynamics and function for a diverse array of protein complexes. We aim to connect high-resolution static images of protein complexes to their movements in an aqueous environment. We want to understand how these movements play a role in either catalysis or binding events. Uncovering the molecular details of protein function will improve our understanding of important biological systems, ultimately facilitating our ability to imitate and interfere with such systems. Specific areas of interest are:

• Macromolecular protein complexes that influence chromatin dynamics during transcription.
• Enzymes with allosteric regulation.
• Continued expansion of the HDX tool box.