title: [Staged equilibrium of carbonic anhydrase unfolding in strong denaturants].
abstract: It has been shown by 1H-NMR, circular dichroism, fluorescence and viscometry techniques that equilibrium unfolding of carbonic anhydrase B (a one-domain globular protein) in urea guanidine hydrochloride consists of two sequential stages. The first stage is connected with a decrease of intramolecular interactions, stabilizing the rigid tertiary structure and with the increase of mobility of aliphatic side chain groups. At the second stage the decrease of protein secondary structure and hydrophobic interactions take place as well as the increase of mobility of massive aromatic side chain groups.
authors.forename: N A
authors.initials: NA
authors.lastname: Rodionova
authors.forename: G V
authors.initials: GV
authors.lastname: Semisotnov
authors.forename: V P
authors.initials: VP
authors.lastname: Kutyshenko
authors.forename: V N
authors.initials: VN
authors.lastname: Uverskiĭ
authors.forename: I A
authors.initials: IA
authors.lastname: Bolotina
mesh_terms: D002256:Carbonic Anhydrases / Q000378:metabolism*; D002942:Circular Dichroism; D006801:Humans; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence; D014508:Urea
chemical_list: D007202:Indicators and Reagents; D014508:Urea; D002256:Carbonic Anhydrases
vernacular_title: Stadiĭnost' ravnovesnogo razvorachivaniia karboangidrazy v sil'nymi denaturantami.