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homooctamer
8 * 60000, SDS-PAGE, AtPGDH2 forms an equilibrium of homooctamers and homotetramers
monomer
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1 * 35000 at pH 5.0
?
x * 50000, SDS-PAGE
?
x * 47700, calculated from amino acid sequence
?
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x * 50000, SDS-PAGE
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?
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x * 47700, calculated from amino acid sequence
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?
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x * 66453 and 90000, DNA sequence analysis and SDS-PAGE
?
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x * 59000, SDS-PAGE
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dimer
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mutant enzyme SerADELTA197
dimer
2 * 33500, calculation from nucleotide sequence
homodimer
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2 * 35000, SDS-PAGE
homodimer
x-ray crystallography
homodimer
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2 * 35000 at pH 7.0
homodimer
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gel filtration
homotetramer
4 * 60000, SDS-PAGE
homotetramer
4 * 60000, SDS-PAGE, AtPGDH2 forms an equilibrium of homooctamers and homotetramers
homotetramer
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4 * 57200, calculated from amino acid sequence
homotetramer
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4 * 57200, calculated from amino acid sequence
homotetramer
4 * 60000, SDS-PAGE
homotetramer
4 * 55000, calculated from amino acid sequence
tetramer
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gel filtration
tetramer
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wild-type enzyme
tetramer
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4 * 40000-50000, sedimentation equilibrium in guanidine-HCl
tetramer
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4 * 44000, SDS-PAGE, each subunit is divided into 3 separate domains
tetramer
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4 * 40000-43000, SDS-PAGE, sedimentation equilibrium studies in guanidine hydrochloride
tetramer
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although the tetramer is composed of identical subunits, significant asymmetry is seen in the tertiary structure of the subunits
tetramer
intervening domains are the two four-stranded beta-sheet structures located next to the substrate binding domains and below the regulatory domains, structure model, overview
tetramer
ligand-bound enzyme, sequence comparison
tetramer
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ligand-bound enzyme, sequence comparison
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tetramer
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intervening domains are the two four-stranded beta-sheet structures located next to the substrate binding domains and below the regulatory domains, structure model, overview
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tetramer
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4 * 60000, SDS-PAGE
additional information
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subunit structure with substrate binding domain, coenzyme binding domain and regulatory domain, active sites
additional information
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subunit structure with substrate binding domain, coenzyme binding domain and regulatory domain, active sites
additional information
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subunit structure with substrate binding domain, coenzyme binding domain and regulatory domain, active sites
additional information
quarternary structure of the active enzyme, conformational changes through domain-domain reorientation, stereochemical model, overview
additional information
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quarternary structure of the active enzyme, conformational changes through domain-domain reorientation, stereochemical model, overview
additional information
the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism
additional information
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the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism
additional information
the enzyme contains an ACT regulatory domain, enzyme domain structure
additional information
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the enzyme contains an ACT regulatory domain, enzyme domain structure
additional information
each subunit consists of three distinct domains: a cofactor or nucleotide binding domain, a substrate binding domain, and a regulatory domain. Structural molecular modeling of mutant enzymes, overview
additional information
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each subunit consists of three distinct domains: a cofactor or nucleotide binding domain, a substrate binding domain, and a regulatory domain. Structural molecular modeling of mutant enzymes, overview
additional information
the apo-enzyme shows an extreme asymmetry in the orientation of the domains from one subunit to another. The poly glycine stretch in the loop that contains the locus for the 160° rotation leads to subunit asymmetry, structure modelling, overview
additional information
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the apo-enzyme shows an extreme asymmetry in the orientation of the domains from one subunit to another. The poly glycine stretch in the loop that contains the locus for the 160° rotation leads to subunit asymmetry, structure modelling, overview
additional information
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the apo-enzyme shows an extreme asymmetry in the orientation of the domains from one subunit to another. The poly glycine stretch in the loop that contains the locus for the 160° rotation leads to subunit asymmetry, structure modelling, overview
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