Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.
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Prediction of solvent accessibility and sites of deleterious mutations from protein sequence.Two monomers of yeast transcription factor ADR1 bind a palindromic sequence symmetrically to activate ADH2 expression.A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genesFunctional characterization of thermolabile DNA-binding proteins that affect adenovirus DNA replication.A procedure for the prediction of temperature-sensitive mutants of a globular protein based solely on the amino acid sequence.Decision making at a subcellular level determines the outcome of bacteriophage infection.Slowing down downhill folding: a three-probe study.Revisiting the myths of protein interior: studying proteins with mass-fractal hydrophobicity-fractal and polarizability-fractal dimensionsTSpred: a web server for the rational design of temperature-sensitive mutantsDNA sequence determinants of lambda repressor binding in vivo.Mutant lambda repressors with increased operator affinities reveal new, specific protein-DNA contacts.A gyrase mutant with low activity disrupts supercoiling at the replication terminusHydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.Protein-Protein Interactions in DNA Recognition: H-NMR Studies of Lambda cI Repressors Genetically Altered by Site-Directed MutagenesisLambda repressor recognizes the approximately 2-fold symmetric half-operator sequences asymmetrically.Regulation of sexual dimorphism: mutational and chemogenetic analysis of the doublesex DM domainHydrophobic packing in T4 lysozyme probed by cavity-filling mutantsLysogen stability is determined by the frequency of activity bursts from the fate-determining genePurification and characterization of a cam repressor (CamR) for the cytochrome P-450cam hydroxylase operon on the Pseudomonas putida CAM plasmidIsotope-detected 1H NMR studies of proteins: a general strategy for editing interproton nuclear Overhauser effects by heteronuclear decoupling, with application to phage lambda repressor.Mutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operonRelative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits.Temperature-sensitive mutations in the bacteriophage Mu c repressor locate a 63-amino-acid DNA-binding domain.A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase.Model of specific complex between catabolite gene activator protein and B-DNA suggested by electrostatic complementarity.Single amino acid substitutions uncouple the DNA binding and strand scission activities of Fok I endonuclease.Isolation and characterization of mutations in the HXK2 gene of Saccharomyces cerevisiae.Genetic identification of the DNA binding domain of Escherichia coli LexA protein.Bacteriophage lambda cro mutations: effects on activity and intracellular degradation.Dominant negative mutations in the Tn10 tet repressor: evidence for use of the conserved helix-turn-helix motif in DNA binding.Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor.Dynamic filtering by two-dimensional 1H NMR with application to phage lambda repressor.Molecular basis of DNA sequence recognition by the catabolite gene activator protein: detailed inferences from three mutations that alter DNA sequence specificity.Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence.Mutational studies with the trp repressor of Escherichia coli support the helix-turn-helix model of repressor recognition of operator DNA.Structure of proteins with single-site mutations: a minimum perturbation approach.NH2-terminal arm of phage lambda repressor contributes energy and specificity to repressor binding and determines the effects of operator mutations.Decision making in living cells: lessons from a simple system.Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding.Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs.
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P2860
Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Mutations in lambda repressor' ...... ein stability and DNA binding.
@en
Mutations in lambda repressor' ...... ein stability and DNA binding.
@nl
type
label
Mutations in lambda repressor' ...... ein stability and DNA binding.
@en
Mutations in lambda repressor' ...... ein stability and DNA binding.
@nl
prefLabel
Mutations in lambda repressor' ...... ein stability and DNA binding.
@en
Mutations in lambda repressor' ...... ein stability and DNA binding.
@nl
P2093
P2860
P356
P1476
Mutations in lambda repressor' ...... ein stability and DNA binding.
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.9.2676
P407
P577
1983-05-01T00:00:00Z