Folding and activity of circularly permuted forms of a polytopic membrane protein.
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The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor.Expression, purification, crystallization and preliminary X-ray analysis of the EIICGlc domain of the Escherichia coli glucose transporterCarbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS).An empirical test of convergent evolution in rhodopsins.Membrane topology of the multidrug transporter MdfA: complementary gene fusion studies reveal a nonessential C-terminal domain.
P2860
Folding and activity of circularly permuted forms of a polytopic membrane protein.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 2000
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@en
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@nl
type
label
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@en
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@nl
prefLabel
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@en
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@nl
P2093
P2860
P356
P1476
Folding and activity of circularly permuted forms of a polytopic membrane protein.
@en
P2093
P2860
P304
P356
10.1073/PNAS.0305463397
P407
P577
2000-02-01T00:00:00Z