Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helices IV and V that contain the major determinants for substrate binding.
about
Positioning of proteins in membranes: a computational approachCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognitionAn approach to membrane protein structure without crystals.Site-directed alkylation and the alternating access model for LacY.The ABC transporter MsbA interacts with lipid A and amphipathic drugs at different sitesSurface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking.Changing the lactose permease of Escherichia coli into a galactose-specific symporterProbing the periplasmic-open state of lactose permease in response to sugar binding and proton translocationStructure and function of the reduced folate carrier a paradigm of a major facilitator superfamily mammalian nutrient transporter.Sugar binding and protein conformational changes in lactose permeaseThe lactose permease of Escherichia coli: overall structure, the sugar-binding site and the alternating access model for transport.Lessons from lactose permeaseStructural conservation in the major facilitator superfamily as revealed by comparative modeling.How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaAqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.Structural basis of substrate selectivity in the glycerol-3-phosphate: phosphate antiporter GlpT.Site-directed alkylation of cysteine to test solvent accessibility of membrane proteins.Residues gating the periplasmic pathway of LacY.Characterization of a cysteine-less human reduced folate carrier: localization of a substrate-binding domain by cysteine-scanning mutagenesis and cysteine accessibility methods.Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry.Site-directed alkylation of LacY: effect of the proton electrochemical gradient.Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport.Probing the mechanism of a membrane transport protein with affinity inactivators.Aqueous access channels in subunit a of rotary ATP synthase.Combining modelling and mutagenesis studies of synaptic vesicle protein 2A to identify a series of residues involved in racetam binding.Dynamic Lipid-dependent Modulation of Protein Topology by Post-translational Phosphorylation.Determinants of substrate recognition by the Escherichia coli multidrug transporter MdfA identified on both sides of the membrane.
P2860
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P2860
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helices IV and V that contain the major determinants for substrate binding.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Site-directed sulfhydryl label ...... minants for substrate binding.
@ast
Site-directed sulfhydryl label ...... minants for substrate binding.
@en
Site-directed sulfhydryl label ...... minants for substrate binding.
@nl
type
label
Site-directed sulfhydryl label ...... minants for substrate binding.
@ast
Site-directed sulfhydryl label ...... minants for substrate binding.
@en
Site-directed sulfhydryl label ...... minants for substrate binding.
@nl
prefLabel
Site-directed sulfhydryl label ...... minants for substrate binding.
@ast
Site-directed sulfhydryl label ...... minants for substrate binding.
@en
Site-directed sulfhydryl label ...... minants for substrate binding.
@nl
P2093
P356
P1433
P1476
Site-directed sulfhydryl label ...... minants for substrate binding.
@en
P2093
P304
10491-10499
P356
10.1021/BI010866X
P407
P577
2001-09-01T00:00:00Z