Structure, Dynamics and Interactions of Proteins

Research overview

My laboratory utilizes high-resolution nuclear magnetic resonance (NMR) spectroscopy and other biophysical and biochemical methods to investigate the structure, dynamics, and folding mechanisms of proteins and to map their functional interactions. NMR is unique as a method for determining three-dimensional structures of proteins and protein complexes in solution and also providing novel information about the time-dependent structural fluctuations that are essential for protein function.

Our research interests include:
• Intrinsically disordered proteins and cellular signaling.
• Mechanisms of nucleic acid recognition by zinc fingers.
• Mechanisms of protein folding and misfolding.
• Protein dynamics and “invisible” excited states.

> Read more about our research