Study of conformational changes in bovine serum albumin by perturbed angular correlations

Abstract The technique of perturbed angular correlations has been used to study the molecular dynamics and conformational changes in bovine serum albumin in aqueous solution using 111 In as a label. The perturbation factors G 2 ( t ) were measured as a function of pH and theoretical fits to these data yield values for quadrupole interaction parameters and rotational correlation times. The data suggest a high degree of local flexibility at the site of the indium label.