The stereochemistry and biochemistry of the trp repressor-operator complex.
about
The tryptophan repressor sequence is highly conserved among the EnterobacteriaceaeStructure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificityA negative electrostatic determinant mediates the association between the Escherichia coli trp repressor and its operator DNA.In vivo and in vitro studies of Chlamydia trachomatis TrpR:DNA interactionsThe DNA target of the trp repressorCooperative folding units of escherichia coli tryptophan repressor.Probing the TRAP-RNA interaction with nucleoside analogs.Substitutions of Thr30 provide mechanistic insight into tryptophan-mediated activation of TRAP binding to RNA.The NH2-terminal arms of trp repressor participate in repressor/operator association.Functional characterization of a replication initiator proteinA stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNAAllosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.Structural aspects of protein-DNA recognition.Mutagenesis supports water mediated recognition in the trp repressor-operator system.The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotide. NMR studies using selectively 15N-labelled protein.The Met repressor-operator complex: DNA recognition by beta-strands.Structure-function correlation for the EcoRV restriction enzyme: from non-specific binding to specific DNA cleavage.The challenge-phage assay reveals differences in the binding equilibria of mutant Escherichia coli Trp super-repressors in vivo.NMR evidence for the RNA stem-loop structure involved in the transcription attenuation of E. coli trp operon.Analysis of trp repressor-DNA interactions using gel electrophoresis.Molecular and biological constraints on ligand-binding affinity and specificity.1H-NMR characterization of L-tryptophan binding to TRAP, the trp RNA-binding attenuation protein of Bacillus subtilisMutants of Escherichia coli Trp repressor with changes of conserved, helix-turn-helix residue threonine 81 have altered DNA-binding specificities.Specific purine N7-nitrogens are critical for high affinity binding by the trp repressor.Statistical mechanical treatment of the structural hydration of biological macromolecules: Results forB-DNANMR Studies of the Mode of Binding of Corepressors and Inducers to Escherichia coli Trp Repressor
P2860
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P2860
The stereochemistry and biochemistry of the trp repressor-operator complex.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artículo científico
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name
The stereochemistry and biochemistry of the trp repressor-operator complex.
@en
The stereochemistry and biochemistry of the trp repressor-operator complex.
@nl
type
label
The stereochemistry and biochemistry of the trp repressor-operator complex.
@en
The stereochemistry and biochemistry of the trp repressor-operator complex.
@nl
prefLabel
The stereochemistry and biochemistry of the trp repressor-operator complex.
@en
The stereochemistry and biochemistry of the trp repressor-operator complex.
@nl
P1476
The stereochemistry and biochemistry of the trp repressor-operator complex.
@en
P2093
P304
P356
10.1016/0167-4781(90)90047-6
P407
P577
1990-04-01T00:00:00Z