Purification, reconstitution, and characterization of the lac permease of Escherichia coli.
about
Lactose permease and the alternating access mechanismComparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes.The kamikaze approach to membrane transportTime-resolved study of the inner space of lactose permeaseEngineering a terbium-binding site into an integral membrane protein for luminescence energy transfer.Substrate-induced changes in the structural properties of LacYSite-directed alkylation and the alternating access model for LacY.Distance determination in proteins using designed metal ion binding sites and site-directed spin labeling: application to the lactose permease of Escherichia coli.An Asymmetric Conformational Change in LacY.Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane.Structure-function relationships of integral membrane proteins: membrane transporters vs channels.Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid compositionOpening the periplasmic cavity in lactose permease is the limiting step for sugar binding.Characterization and functional reconstitution of a soluble form of the hydrophobic membrane protein lac permease from Escherichia coli.Arginine transport in Streptococcus lactis is catalyzed by a cationic exchangerThe central cytoplasmic loop of the major facilitator superfamily of transport proteins governs efficient membrane insertion.Observing a lipid-dependent alteration in single lactose permeasesConformational flexibility at the substrate binding site in the lactose permease of Escherichia coli.Evidence for an intermediate conformational state of LacY.Reconstitution of energy-linked activities of the solubilized F1F0 ATP synthase from Bacillus subtilisRole of the irreplaceable residues in the LacY alternating access mechanismA molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coli.Role of protons in sugar binding to LacYThe lipid bilayer determines helical tilt angle and function in lactose permease of Escherichia coli.Membrane insertion of uracil permease, a polytopic yeast plasma membrane protein.Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation.The purified Bacillus subtilis tetracycline efflux protein TetA(L) reconstitutes both tetracycline-cobalt/H+ and Na+(K+)/H+ exchange.A general method for determining helix packing in membrane proteins in situ: helices I and II are close to helix VII in the lactose permease of Escherichia coli.Electrophysiological characterization of LacY.Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli.YidC assists the stepwise and stochastic folding of membrane proteinsEscherichia coli kgtP encodes an alpha-ketoglutarate transporter.Design of a membrane transport protein for fluorescence spectroscopy.The alternating access transport mechanism in LacY.Ligand-induced conformational changes in the lactose permease of Escherichia coli: evidence for two binding sitesA conformational change in the lactose permease of Escherichia coli is induced by ligand binding or membrane potential.Maltose/proton co-transport in Saccharomyces cerevisiae. Comparative study with cells and plasma membrane vesiclesDelineating electrogenic reactions during lactose/H+ symportResidues gating the periplasmic pathway of LacY.
P2860
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P2860
Purification, reconstitution, and characterization of the lac permease of Escherichia coli.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh
1986年學術文章
@zh-hant
name
Purification, reconstitution, ...... permease of Escherichia coli.
@en
Purification, reconstitution, ...... permease of Escherichia coli.
@nl
type
label
Purification, reconstitution, ...... permease of Escherichia coli.
@en
Purification, reconstitution, ...... permease of Escherichia coli.
@nl
prefLabel
Purification, reconstitution, ...... permease of Escherichia coli.
@en
Purification, reconstitution, ...... permease of Escherichia coli.
@nl
P2093
P1476
Purification, reconstitution, ...... permease of Escherichia coli.
@en
P2093
P304
P356
10.1016/S0076-6879(86)25034-X
P407
P577
1986-01-01T00:00:00Z