Salting-in effects offset MgCL(2)-induced refolding of nucleoside diphosphate kinase.
Previously we reported that halobacterial nucleoside diphosphate kinase can be refolded in the presence of concentrated trimethylamine N-oxide (TMAO) as well as NaCl, indicating that enhancement of compact structure formation by TMAO is sufficient for folding. Here we showed that the refolding effect of MgCl(2) is maximal at 1 M and declines to zero at 2 M, indicating that charge shielding effect of MgCl(2) is offset by its salting-in effect.
Ishibashi
Matsujiro
M
Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
Arakawa
Tsutomu
T
Tokunaga
Masao
M
D019617:Halobacterium salinarum; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D015636:Magnesium Chloride / Q000737:chemistry*; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry*; D009994:Osmolar Concentration; D011489:Protein Denaturation; D017510:Protein Folding; D012492:Salts / Q000737:chemistry*; D012997:Solvents
D012492:Salts; D012997:Solvents; D015636:Magnesium Chloride; D009701:Nucleoside-Diphosphate Kinase