Abstract
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 MgCl2 is maximal at 1 M and declines to zero at 2 M, indicating that charge shielding effect of MgCl2 is offset by its salting-in effect.
Keywords: halophilic, nucleoside diphosphate kinase, refolding, charge shielding, salting-in
Protein & Peptide Letters
Title: Salting-In Effects offset Mgcl2-Induced Refolding of Nucleoside Diphosphate Kinase
Volume: 10 Issue: 6
Author(s): Matsujiro Ishibashi, Tsutomu Arakawa and Masao Tokunaga
Affiliation:
Keywords: halophilic, nucleoside diphosphate kinase, refolding, charge shielding, salting-in
Abstract: 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 MgCl2 is maximal at 1 M and declines to zero at 2 M, indicating that charge shielding effect of MgCl2 is offset by its salting-in effect.
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Cite this article as:
Ishibashi Matsujiro, Arakawa Tsutomu and Tokunaga Masao, Salting-In Effects offset Mgcl2-Induced Refolding of Nucleoside Diphosphate Kinase, Protein & Peptide Letters 2003; 10 (6) . https://dx.doi.org/10.2174/0929866033478546
DOI https://dx.doi.org/10.2174/0929866033478546 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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