Release factors eRF1 and RF2: A universal mechanism controls the large conformational changes

Journal of Biological Chemistry

Volumn 279, Issue 51, 2004, Pages 53875-53885

  Ma, Buyong ^a   Nussinov, Ruth ^a,b  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTER SIMULATION; CONFORMATIONS; ELECTRON MICROSCOPY; ELECTROSTATICS; MOLECULAR DYNAMICS; SYNTHESIS (CHEMICAL);

CRYOELECTRON MICROSCOPY; HISTIDINES; PROTONATION; RIBOSOME;

PROTEINS;

ELONGATION FACTOR G; ELONGATION FACTOR TU; HISTIDINE; RELEASE FACTOR 1; RELEASE FACTOR 2; RELEASING FACTOR; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTON TRANSPORT; RIBOSOME; SIMULATION; SOLVATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HISTIDINE; HUMANS; MODELS, MOLECULAR; MODELS, STATISTICAL; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTOR TU; PEPTIDE TERMINATION FACTORS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RIBOSOMES; RNA, TRANSFER; SEQUENCE HOMOLOGY, AMINO ACID; SOFTWARE; SPECIES SPECIFICITY; THERMODYNAMICS;

EID: 11144223549     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M407412200     Document Type: Article

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