Protein–solvent and weak protein–protein interactions in halophilic malate dehydrogenase
- 15 January 1999
- journal article
- Published by Elsevier in Journal of Crystal Growth
- Vol. 196 (2-4), 395-402
- https://doi.org/10.1016/s0022-0248(98)00822-7
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Mutation at a Single Acidic Amino Acid Enhances the Halophilic Behaviour of Malate Dehydrogenase from Haloarcula Marismortui in Physiological SaltsEuropean Journal of Biochemistry, 1995
- Solution structure of glyceraldehyde-3-phosphate dehydrogenase from Haloarcula vallismortisBiophysical Chemistry, 1995
- Structural Features That Stabilize Halophilic Malate Dehydrogenase from an ArchaebacteriumScience, 1995
- Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortuiBiochemistry, 1993
- Biophysical study of halophilic malate dehydrogenase in solution: revised subunit structure and solvent interactions of native and recombinant enzymeJournal of the Chemical Society, Faraday Transactions, 1993
- Biochemical, Structural, and Molecular Genetic Aspects of HalophilismAdvances in protein chemistry, 1992
- Polypeptide elongation factor Tu from Halobacterium marismortuiEuropean Journal of Biochemistry, 1988
- Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structureBiochemistry, 1977
- Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterizationBiochemistry, 1977
- Salt-dependent properties of proteins from extremely halophilic bacteriaMicrobiology and Molecular Biology Reviews, 1974