| Literature DB >> 6420185 |
D A Dolgikh, A P Kolomiets, I A Bolotina, O B Ptitsyn.
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 alpha-lactalbumins and bovine carbonic anhydrase B.Entities:
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Year: 1984 PMID: 6420185 DOI: 10.1016/0014-5793(84)80020-4
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124