The acquisition of the most stable and biologically active native structure from a completely or partially unfolded state is called as “protein folding”. But “protein folding” process is regulated by complicated cellular environment components like temperature, salt ions, chaperones, crowding agents, pH, solvent etc.and also by the interaction of protein with ligand [includes other macromolecule as peptides/proteins/lipids/carbohydrates/nucleic acids or mixed molecular species thereof as well as small synthetic molecules]. Due to several factors, protein folding process is itself an unsolved puzzle.

In this section, we have focused to investigate the effect of small additives (including dye, drug, nanoparticle etc.) as well as cellular components (different salts and macromolecular crowders that are available in cytoplasmic environment) on protein folding in terms of their conformation, stability, dynamics and kinetics. For this study we are using different optical methods such as Fluorescence, absorption, circular dichroism spectroscopy etc. along with computational approaches.

This study may help us to solve unresolved questions related with protein folding process in the presence of small synthetic molecules as well as cellular constituents.

Reference:

S. Millan, L. Satish, S. Kesh, YS Chaudhary & H. Sahoo*, Interaction of Lysozyme with Rhodamine B: A Cmbined Analysis of Spectroscopic & Molecular Docking, Journal of Photochemistry and Photobiology B, 2016, 162, 248-257.