Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
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Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the proteinCumulative effect of amino acid replacements results in enhanced thermostability of potato type L alpha-glucan phosphorylase.
P2860
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
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Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@en
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@nl
type
label
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@en
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@nl
prefLabel
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@en
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@nl
P2093
P2860
P356
P1433
P1476
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
@en
P2093
Griessler R
Nidetzky B
Schinzel R
P2860
P304
P356
10.1042/BJ3460255
P407
P478
P577
2000-03-01T00:00:00Z