Salting-in effects offset MgCL(2)-induced refolding of nucleoside diphosphate kinase.

Salting-in effects offset MgCL(2)-induced refolding of nucleoside diphosphate kinase.
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盐溶效应抵消了 MgCL(2) 诱导的核苷二磷酸激酶的重折叠。

DOI:
10.2174/0929866033478546
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发表时间:
2003
影响因子:
1.6
通讯作者:
M. Tokunaga
M. Tokunaga
中科院分区:
生物学4区
文献类型:
--
作者:
M. Ishibashi;T. Arakawa;M. Tokunaga

文献摘要

被引文献

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以前,我们报道,盐细菌核苷二磷酸激酶可以在浓缩的三甲基胺N-氧化物(TMAO)以及NaCl的存在下重折叠,表明TMAO的紧凑结构的形成的增强是足够的折叠。在这里,我们发现MgCl(2)的重折叠效应在1 M时最大,在2 M时下降到零,表明MgCl(2)的电荷屏蔽效应被其盐溶效应抵消。
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.