Back in high school, I was taught DNA transcribes into RNA which later translates to protein, the so-called "The Building Block of Life". As I step into college, I realized my teachers forgot to teach me the third and most important process "The Protein Folding" that defines the fate of the protein function. The biological function of a protein relies on the correct folding of its linear amino-acid chain; whereas aberrant folding is often associated with the disease. For example, several unnerving human diseases such as Alzheimer's disease, Parkinson's disease, prion disease, etc. are associated with protein misfolding and aggregation. In the past, I was motivated to unravel the mechanistic and structural basis of protein misfolding and disease progression at a molecular level in a membrane interface. My research was unidirectional (misfolding --> disease) until I explored the natural evolution of "protein intrinsic disorder " and its biological role.  My current research focuses on exploring the physiological function of a few tiny disordered human proteins in the context of their interaction with functional nucleic acid structures such as G-quadruplexes and i-motifs. 

Research Interest:  Protein Misfolding, Membrane Biophysics, Biomolecular Condensates, and G-quadruplex Biology

Technical Expertise: NMR, AUC, CD, FTIR, UV, Fluorescence, ITC, MST, DSC, DLS, Microscopy, AFM, TEM, Chromatography, and Biomolecular modeling and simulation