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Formation of local asymmetric structures in the slow folding reaction of human carbonic anhydrase II Dick Andersson, IFM Chemistry Linkopings University S-581 83 SWEDEN In the study of protein folding we use human carbonic anhydrase II (HCA II) as a model protein. Circular dichroism (CD) and fluorescence have been used to monitor the folding process in engineered tryptophan mutants of HCA II. CD kinetic measurements on engineered tryptophan mutants of HCA II in the near- UV region have been used to probe the development of asymmetric environments around specific Trp residues during the refolding of HCA II. The formation of the active site was probed by the binding of a fluorescent sulfonamide inhibitor. So far three of the seven Trp residues in HCA II have been analyzed. The three selected Trp residues are situated in different sites of the protein and they are the major contributors to the near-UV CD spectrum. The aim of the study is to describe the formation of specific native structures around individual sites during the refolding process of HCA II. The refolding kinetics for the studied Trp residues shows that the asymmetric environment around these Trp residues is formed at different rates, showing that the formation of native-like tertiary structure occurs with varying rates in different regions of the protein. ## Back to the list of abstracts