Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold.
about
Structural consequences of replacement of an alpha-helical Pro residue in Escherichia coli thioredoxinSolution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug designProbing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxinRedox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria.Combinatorial library of improved peptide aptamers, CLIPs to inhibit RAGE signal transduction in mammalian cells.Construction of a catalytically active iron superoxide dismutase by rational protein design.The rational design and construction of a cuboidal iron-sulfur protein.NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A variant: cis/trans peptide isomerizationFolding subdomains of thioredoxin characterized by native-state hydrogen exchangeThe origami of thioredoxin-like folds.Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein.Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile.The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions.Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopyProtein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function.Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin.Real-time kinetics of the interaction between the two subunits, Escherichia coli thioredoxin and gene 5 protein of phage T7 DNA polymerase.Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro.Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein.Simple techniques for the quantification of protein secondary structure by1H NMR spectroscopyReplacement of Trp inEscherichia coliThioredoxin by Site-directed Mutagenesis Affects Thermodynamic Stability but Not Function
P2860
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P2860
Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
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1989年學術文章
@yue
1989年學術文章
@zh-hant
name
Assignment of the proton NMR s ...... ry structure, and global fold.
@en
Assignment of the proton NMR s ...... ry structure, and global fold.
@nl
type
label
Assignment of the proton NMR s ...... ry structure, and global fold.
@en
Assignment of the proton NMR s ...... ry structure, and global fold.
@nl
prefLabel
Assignment of the proton NMR s ...... ry structure, and global fold.
@en
Assignment of the proton NMR s ...... ry structure, and global fold.
@nl
P356
P1433
P1476
Assignment of the proton NMR s ...... ry structure, and global fold.
@en
P2093
P304
P356
10.1021/BI00443A044
P407
P577
1989-08-01T00:00:00Z