Two-state allosteric modeling suggests protein equilibrium as an integral component for cyclic AMP (cAMP) specificity in the cAMP receptor protein of Escherichia coli

Journal of Bacteriology

Volumn 190, Issue 13, 2008, Pages 4532-4540

  Youn, Hwan ^a   Koh, Junseock ^a   Roberts, Gary P ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; CYCLIC AMP; CYCLIC AMP BINDING PROTEIN;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; WILD TYPE;

ADENOSINE; ALLOSTERIC REGULATION; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYCLIC AMP; CYCLIC AMP RECEPTOR PROTEIN; CYCLIC GMP; ESCHERICHIA COLI; MODELS, THEORETICAL; PROTEIN BINDING; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 46049099791     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00074-08     Document Type: Article

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