Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: stability and binding properties
- 14 January 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 295 (2), 279-288
- https://doi.org/10.1006/jmbi.1999.3367
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Stability and Folding of Dihydrofolate Reductase from the Hyperthermophilic Bacterium Thermotoga maritima,Biochemistry, 1999
- Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedProtein Science, 1999
- The stability of proteins in extreme environmentsCurrent Opinion in Structural Biology, 1998
- Recombinant phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima : catalytic, spectral and thermodynamic properties 1 1Edited by R. HuberJournal of Molecular Biology, 1998
- Thermodynamic Characterization of the Reversible, Two-State Unfolding of Maltose Binding Protein, a Large Two-Domain ProteinBiochemistry, 1997
- Structure and Stability of Hyperstable Proteins: Glycolytic Enzymes From Hyperthermophilic Bacterium Thermotoga MaritimaAdvances in protein chemistry, 1996
- Interaction of SecB with intermediates along the folding pathway of maltose‐binding proteinProtein Science, 1995
- UV difference spectroscopy of ligand binding to maltose‐binding proteinFEBS Letters, 1992
- Protein stability and molecular adaptation to extreme conditonsEuropean Journal of Biochemistry, 1991
- Tritium NMR spectroscopy of ligand binding to maltose-binding proteinBiochemistry, 1991