2-STAGE EQUILIBRIUM UNFOLDING OF CARBOANHYDRASE B BY STRONG DENATURING AGENTS

Google Scholar
  • 1 May 1989
    • journal article
    • research article
    • Vol. 23  (3) , 528-536
Abstract
It has been shown by 1H-NMR, circular dichroism, fluorescence an 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 interaction take place as well as the increase of mobility of massive aromatic side chain groups.