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• W2012121208 endingPage "10305" @default.
• W2012121208 startingPage "10295" @default.
• W2012121208 abstract "We have synthesized two 40 base pair DNA fragments; one fragment contains the consensus DNA site for CAP (fragment 'ICAP'); the other fragment contains the E. coli lac promoter DNA site for CAP (fragment 'LCAP'). We have investigated the binding of CAP to the two DNA fragments using the nitrocellulose filter binding assay. Under standard conditions [( NaCl] = 200 mM, pH = 7.3), CAP exhibits a 450-fold higher affinity for ICAP than for LCAP. The salt dependence of the binding equilibrium indicates that CAP makes eight ion pairs with ICAP, but only six ion pairs with LCAP. Approximately half of the difference in binding free energy for interaction of CAP with ICAP vs. LCAP is attributable to this difference in ion-pair formation. The pH dependence of the binding equilibrium indicates that the eight CAP-ICAP ion pairs and the six CAP-LCAP ion pairs do not involve His residues of CAP." @default.
• W2012121208 created "2016-06-24" @default.
• W2012121208 creator A5075594154 @default.
• W2012121208 creator A5087284111 @default.
• W2012121208 date "1989-01-01" @default.
• W2012121208 modified "2023-10-13" @default.
• W2012121208 title "Consensus DNA site for the<i>Escherichia coli</i>catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the<i>E.coli lac</i>DNA site" @default.
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• W2012121208 doi "https://doi.org/10.1093/nar/17.24.10295" @default.
• W2012121208 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/335301" @default.
• W2012121208 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2557589" @default.
• W2012121208 hasPublicationYear "1989" @default.
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