@article{GUO2005, 
author = {Xiaogang GUO and Liping XIE and Jicheng PAN and Rongqing ZHANG},
title = {Characteristics of Two Intermediates Trapped in the Unfolding Pathway of Arginine Kinase Induced by Guanidinium Chloride},
year = {2005},
journal = {Tsinghua Science and Technology},
volume = {10},
number = {4},
pages = {461-468},
keywords = {molten globule state, arginine kinase, equilibrium intermediate, partly folded state},
url = {https://www.sciopen.com/article/10.1016/S1007-0214(05)70101-2},
doi = {10.1016/S1007-0214(05)70101-2},
abstract = {Equilibrium guanidinium chloride (GdmCl)-induced unfolding of arginine kinase (AK) was investigated by enzymatic activity, intrinsic fluorescence, 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence, circular dichroism (CD) spectrum, and size-exclusion chromatography. The measurements showed that AK unfolded through two equilibrium intermediates: the molten globule state and the partly folded state. Both intermediates have no enzyme activity. The molten globule state exists at 0.4-0.8 mol/L GdmCl, perhaps after the N-terminal domain has unfolded but the C-terminal domain is still intact. The partly folded state occurs at 1.1-1.5 mol/L GdmCl with a hydrodynamic volume no more than 1.6-fold larger than the native state and a pronounced far UV-CD signal. Its ANS fluorescence intensity is about 50% of the molten globule state. This partly folded state shares similarities with the “burst” kinetic intermediate of protein folding.}
}