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

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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 111In as a label. The perturbation factors G2(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.

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