Sakshi Bhagat – @sakszi
Being the most dynamic component of majority of biological processes solvent plays a crucial role in changing the protein’s conformation in the system. The structural evolution of protein in various media, such as co-solvents, electrolytes, and others indicates existence of various intra- and intermolecular interactions that are responsible for maintaining protein stability. In the present study we focussed on the spin-lattice relaxation of deuterium nuclei present in co-solvents deciphering conformational changes in β-LG at variable concentration of co-solvent at a neutral pH. Β-LG is a milk protein with 162 Amino acids and is found abundantly in milk and is one the most extensively studied β-sheet protein. Presently, tri-fluorethanol (TFE) and Acetonitrile (ACN) are the two organic solvents under investigation. Spin-lattice relaxation rates of 2H nuclei can provide solitary insights into time dependent conformational fluctuation of β-LG from beta sheet to the α-helix structure.
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