Dr. Sunita Patel, Ph.D.

In our startup, my role is to define the strategic direction for our ongoing Neurocare projects, prioritizing precision, safety, and efficiency. I am responsible for identifying problems and challenges, implementing corrective measures, and ensuring the successful achievement of project goals. I allocate specific responsibilities to team members and oversee the validation and assessment of our products. Additionally, I engage with key opinion leaders in the neurodomain to gain insights into their unique needs and requirements, ensuring our solutions are aligned with their expectations.

I studied Crystallin proteins and its mutant using NMR, biophysical methods and replica exchange molecular dynamics simulations. For the study, I took a highly ordered and an intrinsically disordered Crystallin. Interesting insights have been deduced on Crystallin structural stability and dynamics. Aggregation of peptide segment from myoglobin is also studied.

I took teaching responsibility in virtual mode as part of the Institute's academic programs in the course CHM 625 (Biophysical Chemistry).

This is the period during which analyses of protein NMR experiments were carried out on an intrinsically disordered protein Hahellin. REMD simulations were performed and complemented with the result obtained from solution NMR experiments. Besides aggregation of myoglobin peptide was studied using molecular dynamics simulations methods.

I worked extensively in solution NMR during this period. In addition I used molecular dynamics simulation to study various proteins structure and dynamics to understand their functions. NMR assignment was done by recording double- and triple-resonance experiments on an intrinsically disordered protein Hahellin and its dynamics was studied by recording 15N relaxation experiments. The structure calculation and dynamics was also studied for a mutant Y81F-EhCaBP1 from E. histolytica which is an important protein for the etiology of parasite.

I deciphered the most probable conformation of the small heat shock protein (sHSP). Impaired expression and/or mutation of sHSPs are associated with a number of diseases related to protein folding such as Parkinson’s, diffuse Lewy body, Huntington’s and Alzheimer’s disease. Mutations of sHSPs also cause cataract in the eye, muscle myopathies and neuropathies. In addition, altered expression of sHSPs is observed in certain cancers. Understanding the mechanism of sHSP function, therefore, is of considerable interest to many areas of biology and medicine.

Early events in protein folding have been studied using molecular dynamics simulations during this period. Mostly used peptide models from various proteins as it represents a simplistic model system for an unfolded state. Free energy calculation were performed by using first two principal components derived from principal component analyses. The interactions driving protein folding have been identified and deduced.