Molecular strategies to replace the structural metal site in the prokaryotic zinc finger domain

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1844, Issue 3, 2014, Pages 497-504

  Baglivo, Ilaria ^a   Palmieri, Maddalena ^a   Rivellino, Alessia ^a   Netti, Fortuna ^a   Russo, Luigi ^a   Esposito, Sabrina ^a   Iacovino, Rosa ^a   Farina, Biancamaria ^b,c   Isernia, Carla ^a,b   Fattorusso, Roberto ^a,b   Pedone, Paolo Vincenzo ^a,b   Malgieri, Gaetano ^a  

^a Department of Environmental   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c CNR   (Italy)

Author keywords

DNA binding; Prokaryotic zinc finger; Thermal unfolding

Indexed keywords

PROTEIN ML4; PROTEIN ML5; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; HISTIDINE; METAL ION; MI 4 PROTEIN; MI 5 PROTEIN; PROTEIN; BACTERIAL PROTEIN; DNA; METAL;

AGROBACTERIUM TUMEFACIENS; ALPHA HELIX; ARTICLE; BIOINFORMATICS; CARBON NUCLEAR MAGNETIC RESONANCE; DNA BINDING; HYDROGEN BOND; HYDROPHOBICITY; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROKARYOTE; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; THERMOSTABILITY; ZINC FINGER MOTIF; BACTERIAL STRAIN; CONTROLLED STUDY; DELETION MUTANT; ESCHERICHIA COLI; HETERONUCLEAR SINGLE QUANTUM COHERENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; STRUCTURAL BIOINFORMATICS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; GEL MOBILITY SHIFT ASSAY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEAR MAGNETIC RESONANCE; PROKARYOTIC ZINC FINGER; SEQUENCE HOMOLOGY; THERMAL UNFOLDING;

DNA BINDING; PROKARYOTIC ZINC FINGER; THERMAL UNFOLDING;

AGROBACTERIUM TUMEFACIENS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CIRCULAR DICHROISM; DNA; ELECTROPHORETIC MOBILITY SHIFT ASSAY; METALS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SEQUENCE HOMOLOGY, AMINO ACID; ZINC FINGERS;

EID: 84892910209     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.12.019     Document Type: Article

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