The respiratory syncytial virus transcription antiterminator M 2-1 is a highly stable, zinc binding tetramer with strong pH-dependent dissociation and a monomeric unfolding intermediate

Biochemistry

Volumn 50, Issue 40, 2011, Pages 8529-8539

  Esperante, Sebastián A ^a   Chemes, Lucía B ^a   Sánchez, Ignacio E ^b   De Prat Gay, Gonzalo ^a  

^a FUNDACIÓN INSTITUTO LELOIR   (Argentina)

^b UNIVERSIDAD DE BUENOS AIRES   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL PROPERTIES; CELLULAR ENVIRONMENT; CONCENTRATION-DEPENDENT; COOPERATIVE TRANSITIONS; DISSOCIATION CONSTANT; ELONGATION FACTOR; FREE ENERGY CHANGE; GLOBAL FITTING; HIGH IONIC STRENGTH; HYDRODYNAMIC RADIUS; MOLTEN GLOBULE; MONOMERIC INTERMEDIATE; PH RANGE; PH-DEPENDENT; PROTEIN CONCENTRATIONS; REGULATORY EFFECTS; RESPIRATORY SYNCYTIAL VIRUS; RNA POLYMERASE; SECONDARY AND TERTIARY STRUCTURES; STRUCTURAL CHANGE; TETRAMERS; ZINC BINDING; ZINC CONTENT;

DISSOCIATION; EXPERIMENTS; FREE ENERGY; GENES; IONIC STRENGTH; OLIGOMERS; PH EFFECTS; RNA; VIRUSES; ZINC;

TRANSCRIPTION;

MONOMER; PROTEIN M2; PROTEIN M2-1; RNA; RNA POLYMERASE; TETRAMER; UNCLASSIFIED DRUG; VIRUS PROTEIN; ZINC;

ALPHA HELIX; ARTICLE; ATOM; BIOCHEMISTRY; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; HYDRODYNAMICS; IONIC STRENGTH; LIGHT SCATTERING; NONHUMAN; PH; PNEUMOVIRINAE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; REGULATOR GENE; RESPIRATORY SYNCYTIAL PNEUMOVIRUS;

HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; PEPTIDE ELONGATION FACTORS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN UNFOLDING; RESPIRATORY SYNCYTIAL VIRUS INFECTIONS; RESPIRATORY SYNCYTIAL VIRUS, HUMAN; VIRAL PROTEINS; ZINC;

HUMAN RESPIRATORY SYNCYTIAL VIRUS; PARAMYXOVIRIDAE; PNEUMOVIRUS; RESPIRATORY SYNCYTIAL VIRUS;

EID: 80053611065     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200661k     Document Type: Article

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