‘Molten‐globule“ state accumulates in carbonic anhydrase folding

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Abstract
Kinetics of folding and unfolding of bovine carbonic anhydrase B were monitored by circular dichroism, viscometry and esterase activity. It was shown that kinetic intermediate states accumulating in folding process reveal a native‐like compactness and secondary structure but have a symmetrized average environment of aromatic side groups and no esterase activity. These properties allow one to consider these intermediate states as the ‘molten‐globule“ state of a protein molecule previously described by us for several equilibrium forms of bovine and human α‐lactalbumins and bovine carbonic anhydrase B.