PAC studies of BSA conformational changes

The structure of biological molecules plays an important role in many biological processes. The variation of ambient parameters such as pH, temperature or pressure can influence important properties of protein molecules like conformation or stability. By means of the perturbed angular correlation (PAC) technique and atomic force microscopy (AFM) a conformation change of bovine serum albumin (BSA) molecules has been studied as a function of the pH value of the BSA solution. The observed decrease of the rotational correlation time and the increase of molecule diameter as a function of pH were attributed to conformational changes of bovine serum albumin induced by different pH values of the BSA solution.