‘Molten‐globule“ state accumulates in carbonic anhydrase folding

FEBS Letters

Dolgikh, D.A.²  Ptitsyn, O.B.²  Bolotina, I.A.¹  Kolomiets, A.P.² 

[1] Institute of Molecular Biology, USSR Academy of Sciences, 117312 Moscow, USSR;Institute of Protein Research, USSR Academy of Sciences, 142292 Pushchino, Moscow Region, USSR

关键词: Carbonic anhydrase B;    Protein folding;    Molten-globule state of protein molecules;    Folding intermediate;    CA B;    carbonic anhydrase B;    α-LA;    α-lactalbumin;    Gu-HCl;    guanidine hydrochloride;    CD;    circular dichroism;    UV;    ultraviolet;    states of CA B — N (native);    I (intermediate) and U (unfolded);   

DOI  :  10.1016/0014-5793(84)80020-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown