Deceleration of Arginine Kinase Refolding by Induced Helical Structures |
| |
Authors: | Hai-Long Li Sheng-Mei Zhou Daeui Park Hyoung Oh Jeong Hae Young Chung Jun-Mo Yang Fan-Guo Meng Wei-Jiang Hu |
| |
Institution: | (1) Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, 314006, People’s Republic of China;(2) College of Biology and Chemical Engineering, Jiaxing University, Jiaxing, 314000, People’s Republic of China;(3) Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University, Busan, 609-735, Korea;(4) Department of Dermatology, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, 135-710, Korea; |
| |
Abstract: | Arginine kinase (AK) is a key metabolic enzyme for keeping energy balance in invertebrates. Therefore, regulation of the enzymatic
activity and the folding studies of AK from the various invertebrates have been the focus of investigation. We studied the
effects of helical structures by using hexafluoroisopropanol (HFIP) on AK folding. Folding kinetic studies showed that the
folding rates of the urea-denatured AKs were significantly decelerated after being induced in various concentrations of HFIP.
AK lost its activity completely at concentrations greater than 60%. The results indicated that the HFIP-induced helical structures
in the denatured state play a negative role in protein folding, and the helical structures induced in 5% (v/v) HFIP act as
the most effective barrier against AK taking its native structure. The computational docking simulations (binding energies
for −2.19 kcal/mol for AutoDock4.2 and −20.47 kcal/mol for Dock6.3) suggested that HFIP interacts with the several important
residues that are predicted by both programs. The excessively pre-organized helical structures not only hampered the folding
process, but also ultimately brought about changes in the three-dimensional conformation and biological function of AK. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|