In high school, I learned that DNA transcribes into RNA, which then translates into protein—the so-called "building blocks of life." However, it wasn't until college that I unearthed a vital aspect: protein folding. This intricate process shapes the ultimate function of a protein, as its biological activity hinges on the correct folding of its linear amino acid chain. Conversely, protein misfolding is often associated with various human diseases, including 'Diabetes, Alzheimer's disease, Parkinson's disease, and Prion disease'. 

My early research was dedicated to deciphering the mechanistic and structural underpinnings of protein misfolding and its impact on disease progression at the molecular level, particularly at the membrane interface. This approach was initially linear, tracing the path from protein misfolding to disease. Over time, my focus expanded to include the natural evolution of protein intrinsic disorder and its biological significance. 

Currently, my research delves into the physiological functions of small disordered human proteins, with a keen interest in their structural interaction with functional nucleic acid structures such as G-quadruplexes and microRNAs.

Research Interest: Biophysics | Biochemistry | Non-canonical Nucleic Acids | G-quadruplex | Structural Biology | Biomolecular Condensates | Protein Misfolding