Electrostatic interactions across the dimer-dimer interface contribute to the pH-dependent stability of a tetrameric malate dehydrogenase.
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Tetramerization reinforces the dimer interface of MnSODInterface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase.Resolving hot spots in the C-terminal dimerization domain that determine the stability of the molecular chaperone Hsp90Oligomeric interfaces as a tool in drug discovery: Specific interference with activity of malate dehydrogenase of Plasmodium falciparum in vitro.
P2860
Electrostatic interactions across the dimer-dimer interface contribute to the pH-dependent stability of a tetrameric malate dehydrogenase.
description
2003 nî lūn-bûn
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name
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@en
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@nl
type
label
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@en
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@nl
prefLabel
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@en
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@nl
P2093
P2860
P1433
P1476
Electrostatic interactions acr ...... trameric malate dehydrogenase.
@en
P2093
Alexandra Bjørk
Dimitrios Mantzilas
Reidun Sirevåg
P2860
P304
P356
10.1016/S0014-5793(03)01076-7
P407
P577
2003-10-01T00:00:00Z