Using Fluorescence spectroscopy and stopped-flow kinetics, we study the protein folding and refolding dynamics.
Currents projects include:
The change in the stability of SciW and EagT6 chaperones in the presence and absence of transmembrane domain and how key mutations affect the dynamics of refolding.
Salt-induced folding dynamics of intrinsically disordered protein, Paradox and the Hofmeister salt effect on the interaction with a binding partner, ComR.
Hofmeister effects on the tetramerization of melittin as studied through intrinsic tryptophan fluorescence, stopped-flow kinetics, and fluorescence lifetime measurement.