Elastic compliance and adsorption profiles of Bovine serum albumin at fluid/solid interface in the presence of electrolytes.

Non-trivial topology of proteins under shear suggests that even small structural changes in proteins result in dramatic variations in the mechanical properties and stability. In this study, we have analysed the elastic compliance of solvated bovine serum albumin (BSA) with NaCl,MgCl, FeCl of concentration-ranging from 50 mM to 250 mM using Quartz crystal microbalance with dissipation. The compliance shows a reverse Hofmeister trend (Na +