Activation of Halophilic Nucleoside Diphosphate Kinase by a Non-ionic Osmolyte, Trimethylamine N-Oxide
- 1 May 2003
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 22 (4) , 345-351
- https://doi.org/10.1023/a:1025338106922
Abstract
The folding and activity of halophilic enzymes are believed to require the presence of salts at high concentrations. When the inactivated nucleoside diphosphate kinase (NDK) from extremely halophilic...Keywords
This publication has 22 references indexed in Scilit:
- Relative Role of Anions and Cations in the Stabilization of Halophilic Malate DehydrogenaseBiochemistry, 1999
- The Structural Basis of Protein HalophilicityComparative Biochemistry and Physiology Part A: Physiology, 1997
- A Naturally Occurring Protective System in Urea-Rich Cells: Mechanism of Osmolyte Protection of Proteins against Urea DenaturationBiochemistry, 1997
- Correcting temperature-sensitive protein folding defects.Journal of Clinical Investigation, 1997
- Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyolsEnzyme and Microbial Technology, 1996
- NADP-glutamate dehydrogenase from the halophilic archaeonHaloferax mediterraner. enzyme purification, N-terminal sequence and stabilityFEMS Microbiology Letters, 1996
- The Peptide Backbone Plays a Dominant Role in Protein Stabilization by Naturally Occurring OsmolytesBiochemistry, 1995
- Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortuiBiochemistry, 1993
- Preferential interactions of proteins with salts in concentrated solutionsBiochemistry, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970