title: Sequential mechanism of refolding of carbonic anhydrase B.
abstract: 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.
authors.affiliation: Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.
authors.forename: G V
authors.initials: GV
authors.lastname: Semisotnov
authors.forename: N A
authors.initials: NA
authors.lastname: Rodionova
authors.forename: V P
authors.initials: VP
authors.lastname: Kutyshenko
authors.forename: B
authors.initials: B
authors.lastname: Ebert
authors.forename: J
authors.initials: J
authors.lastname: Blanck
authors.forename: O B
authors.initials: OB
authors.lastname: Ptitsyn
mesh_terms: D000818:Animals; D002256:Carbonic Anhydrases; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D005470:Fluorometry; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation
chemical_list: D002256:Carbonic Anhydrases