Calorimetric analysis of the Ca2+-binding βγ-crystallin homolog protein S from Myxococcus xanthus: intrinsic stability and mutual stabilization of domains
- 1 October 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 293 (1) , 117-124
- https://doi.org/10.1006/jmbi.1999.3146
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Kinetic and Thermodynamic Stabilization of the βγ-Crystallin Homolog Spherulin 3a from Physarum polycephalum by Calcium BindingJournal of Molecular Biology, 1999
- The domains of protein S from Myxococcus xanthus: structure, stability and interactionsJournal of Molecular Biology, 1999
- Equilibrium folding intermediates of a greek key β-barrel proteinJournal of Molecular Biology, 1998
- Ca 2+ -loaded spherulin 3a from Physarum polycephalum adopts the prototype γ-crystallin fold in aqueous solution 1 1Edited by P. E. WrightJournal of Molecular Biology, 1997
- Mutational analysis of hydrophobic domain interactions in γB-crystallin from bovine eye lensProtein Science, 1997
- Hyperthermophile Protein Folding Thermodynamics: Differential Scanning Calorimetry and Chemical Denaturation of Sac7dJournal of Molecular Biology, 1996
- High resolution structure of an oligomeric eye lens β-crystallinJournal of Molecular Biology, 1991
- Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteinsJournal of Molecular Evolution, 1990
- Packing interactions in the eye-lensJournal of Molecular Biology, 1989
- Co-operative blocks in tropomyosinJournal of Molecular Biology, 1982