Staged equilibrium of carbonic anhydrase unfolding in strong denaturants
Rodionova, N.A.; Semisotnov, G.V.; Kutyshenko, V.P.; Uverskiĭ, V.N.; Bolotina, I.A.
Molekuliarnaia Biologiia 23(3): 683-692
1989
ISSN/ISBN: 0026-8984 PMID: 2505062 Document Number: 344271
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.