Normal-mode analysis suggests protein flexibility modulation throughout RNA polymerase's functional cycle

Biochemistry

Volumn 43, Issue 41, 2004, Pages 13083-13096

  Van Wynsberghe, Adam ^a   Li, Guohui ^a   Cui, Qiang ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL ATOMIC STRUCTURE; ENZYMES; MATHEMATICAL MODELS; RNA;

ARTIFACTUAL FORCES; BLOCK NORMAL-MODE ANALYSIS (BNM); CRYSTAL PACKING; ELASTIC NETWORK MODEL (ENM);

PROTEINS;

DOUBLE STRANDED DNA; HOLOENZYME; RNA POLYMERASE;

ANALYTIC METHOD; ARTICLE; CALCULATION; COMPLEX FORMATION; ENZYME MECHANISM; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; SEQUENCE HOMOLOGY;

BACTERIAL PROTEINS; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; DNA-DIRECTED RNA POLYMERASES; ELASTICITY; ESCHERICHIA COLI PROTEINS; HOLOENZYMES; MODELS, MOLECULAR; PROTEIN CONFORMATION; SIGMA FACTOR; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; TAQ POLYMERASE; THERMODYNAMICS; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); DECAPODA (CRUSTACEA);

EID: 5444228752     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049738+     Document Type: Article

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