We are broadly interested in studying protein structure and dynamics using biomolecular NMR spectroscopy. In parallel, we will also investigate the physical and conformational changes accompanying complex biomolecular reactions (e.g. protein aggregation) using a variety of biophysical tools. The laboratory will work at the intersection of physical chemistry and structural biology of proteins, using a combination of NMR and other spectroscopic tools, with the help of modern molecular biology and protein biochemistry techniques.
In particular, we will be investigating how long-range interactions (tertiary structure) can tune the local secondary structure of proteins, with the ultimate goal of designing proteins which can reversibly adopt more than one unique fold. This idea has parallels with protein aggregation reactions, which are also often accompanied by drastic conformational changes. More specifically, transient conformational fluctuations in proteins have been hypothesized to initiate protein aggregation and misfolding reactions. We aim to detect these high energy states, modulate their stabilities and lifetimes by protein engineering and binding, and ultimately solve their structures in both the native and the aggregated states.
New Office Automation (Pingala) 
