Sequential mechanism of refolding of carbonic anhydrase B.
The kinetics of refolding of bovine carbonic anhydrase B was studied by a variety of methods over a wide range of times (from milliseconds to hours). It has been shown that protein refolding proceeds through three stages. At the first stage (t1/2 approximately equal to 0.03 s) hydrophobic clusters and a compact state of the chain are formed. At the second stage (t1/2 approximately equal to 140 s) hydrophobic clusters are desolvated and the rigid native-like hydrophobic core is formed. At the third stage (t1/2 approximately equal to 600 s) the native active protein is formed.
Semisotnov
G V
GV
Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.
Rodionova
N A
NA
Kutyshenko
V P
VP
Ebert
B
B
Blanck
J
J
Ptitsyn
O B
OB
D000818:Animals; D002256:Carbonic Anhydrases; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D005470:Fluorometry; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation
D002256:Carbonic Anhydrases