Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
about
Structure-based studies on the metal binding of two-metal-dependent sugar isomerasesThe kamikaze approach to membrane transportA pyrene maleimide with a flexible linker for sampling of longer inter-thiol distances by excimer formationAn approach to membrane protein structure without crystals.Prediction of membrane protein structures with complex topologies using limited constraintsArg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli.Changing the lactose permease of Escherichia coli into a galactose-specific symporterPolar residues drive association of polyleucine transmembrane helicesStructural modeling and electron paramagnetic resonance spectroscopy of the human Na+/H+ exchanger isoform 1, NHE1.Structural model for 12-helix transporters belonging to the major facilitator superfamily.Structural biology and function of solute transporters: implications for identifying and designing substrates.Functional characterization of cysteine residues in GlpT, the glycerol 3-phosphate transporter of Escherichia coliThe lactose permease of Escherichia coli: overall structure, the sugar-binding site and the alternating access model for transport.Conformational flexibility at the substrate binding site in the lactose permease of Escherichia coli.Lactose permease as a paradigm for membrane transport proteins (Review).Lessons from lactose permeaseExploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli.Unraveling the mechanism of the lactose permease of Escherichia coli.Binding affinity of lactose permease is not altered by the H+ electrochemical gradient.The extent of pyrene excimer fluorescence emission is a reflector of distance and flexibility: analysis of the segment linking the LDL receptor-binding and tetramerization domains of apolipoprotein E3.Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease.Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.Probing the mechanism of a membrane transport protein with affinity inactivators.In vitro synthesis of lactose permease to probe the mechanism of membrane insertion and folding.Sugar recognition by the lactose permease of Escherichia coli.Examination of lipid-bound conformation of apolipoprotein E4 by pyrene excimer fluorescence.
P2860
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P2860
Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
@en
type
label
Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
@en
prefLabel
Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
@en
P2093
P356
P1433
P1476
Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
@en
P2093
P304
P356
10.1021/BI9906524
P407
P577
1999-06-01T00:00:00Z