Affiliation: University of Oslo
- Electrostatic interactions across the dimer-dimer interface contribute to the pH-dependent stability of a tetrameric malate dehydrogenaseAlexandra Bjørk
Department of Biology, University of Oslo, Box 1031 Blindern, N 0316 Oslo, Norway
FEBS Lett 553:423-6. 2003..8 degrees C, and depended strongly on pH. Gel-filtration experiments indicated that the 26.8 degrees C loss in stability observed for the D56K mutant at low pH was accompanied by a shift towards a lower oligomerization state...
- Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interfaceAlexandra Bjørk
Department of Biology, University of Oslo, PO Box 1031 Blindern, N 0316 Oslo, Norway
J Mol Biol 334:811-21. 2003..The results show that tetramerization may contribute to MDH stability to an extent that depends strongly on the number of stabilizing interactions in the dimer-dimer interface...
- Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interfaceAlexandra Bjørk
Department of Molecular Biosciences, University of Oslo, P O Box 1041, Blindern, N 0316 Oslo, Norway
J Mol Biol 341:1215-26. 2004....
- Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenasesBjørn Dalhus
Department of Chemistry, University of Oslo, Box 1033, Blindern, N 0316 Oslo, Norway
J Mol Biol 318:707-21. 2002..A structural alignment of tetrameric and dimeric prokaryotic MDHs reveal that structural elements that differ among dimeric and tetrameric MDHs are located in a few loop regions...