Salting-In Effects offset Mgcl2-Induced Refolding of Nucleoside Diphosphate Kinase

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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: charge shielding; halophilic; nucleoside diphosphate kinase; refolding; salting-in

Document Type: Review Article


Affiliations: Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan, and Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA.

Publication date: December 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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