Equilibrium unfolding of yeast triosephosphate isomerase: a monomeric intermediate in guanidine-hci and two-state behavior in urea

Title:Equilibrium unfolding of yeast triosephosphate isomerase: a monomeric intermediate in guanidine-hci and two-state behavior in urea

Volume: 7 Issue: 1

Author(s): Edgar Vazquez-Contreras, Rafael A. Zubillaga, Guillermo Mendoza-Hernandez, Miguel Costast and D. Alejandro Fernandez-Velascot

Affiliation:

Abstract: This is the first experimental evidence of an equilibrium intermediate in the unfolding of triosephosphate isomerase (TIM). The reversible unfolding of S. cerevisiae TIM induced by both guanidine­ HCl (Gdn-HCl) and urea, are apparently monophasic when followed by spectroscopic techniques. Kinetic analysis and ANS binding data confirm a two-state transition in urea. nevertheless, in Gdn-HCl they indicate an intermediate. Hydrodynamic properties of the intermediate are consistent with a compact monomer.

Cite this article as:

Vazquez-Contreras Edgar, Zubillaga A. Rafael, Mendoza-Hernandez Guillermo, Costast Miguel and Fernandez-Velascot Alejandro D., Equilibrium unfolding of yeast triosephosphate isomerase: a monomeric intermediate in guanidine-hci and two-state behavior in urea, Protein & Peptide Letters 2000; 7 (1) . https://dx.doi.org/10.2174/092986650701221205160148