Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.
about
Time-resolved study of the inner space of lactose permeaseThe aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.Alanine insertion scanning mutagenesis of lactose permease transmembrane helices.Distance determination in proteins using designed metal ion binding sites and site-directed spin labeling: application to the lactose permease of Escherichia coli.Changing the lactose permease of Escherichia coli into a galactose-specific symporterA molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coli.Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases.Protein footprinting at cysteines: probing ATP-modulated contacts in cysteine-substitution mutants of yeast DNA topoisomerase II.Determination of the multimerization state of the hepatitis delta virus antigens in vivoFe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domainsA 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.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.Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: structural properties and evidence for a substrate-induced conformational change.Binding of monoclonal antibody 4B1 to homologs of the lactose permease of Escherichia coli.Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry.The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification.Scleroderma autoantigens are uniquely fragmented by metal-catalyzed oxidation reactions: implications for pathogenesisProperties of a cysteine-free proton-pumping nicotinamide nucleotide transhydrogenase.The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis.In vitro synthesis of lactose permease to probe the mechanism of membrane insertion and folding.Inhibition of Oxidative Cross-linking between Engineered Cysteine Residues at Positions 332 in Predicted Transmembrane Segments (TM) 6 and 975 in Predicted TM12 of Human P-glycoprotein by Drug Substrates
P2860
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P2860
Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.
description
1995 nî lūn-bûn
@nan
1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Helix packing of lactose perme ...... te-directed chemical cleavage.
@ast
Helix packing of lactose perme ...... te-directed chemical cleavage.
@en
type
label
Helix packing of lactose perme ...... te-directed chemical cleavage.
@ast
Helix packing of lactose perme ...... te-directed chemical cleavage.
@en
prefLabel
Helix packing of lactose perme ...... te-directed chemical cleavage.
@ast
Helix packing of lactose perme ...... te-directed chemical cleavage.
@en
P2093
P2860
P356
P1476
Helix packing of lactose perme ...... te-directed chemical cleavage.
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.20.9186
P407
P577
1995-09-01T00:00:00Z