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The investigation of ligand binding and subunit exchange in transthyretin (TTR) complexes was discussed. Subunit exchange was followed by mixing equimolar quantities of L55P TTR uniformly labeled with 15N and unlabeled wild type WT to produce a solution with an overall concentration of 10 μM. It was observed that after incubation for 34 mins, separate peaks for the labeled and unlabeled tetramer were no longer visible. It was shown that in the presence of a 3-fold excess of thyroxine the rate of subunit exchange was reduced.


Conference paper

Publication Date



251 - 252