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Petri Dish


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.

Protein Dynamics: Research
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