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• W2111332057 abstract "Differential scanning calorimetry and UV thermal denaturation have been used to determine a complete thermodynamic profile for the bis-intercalative interaction of the peptide antibiotic echinomycin with DNA. The new calorimetric data are consistent with all previously published binding data, and afford the most rigorous and direct determination of the binding enthalpy possible. For the association of echinomycin with DNA, we found DeltaG degrees = -7.6 kcal mol(-1), DeltaH = +3.8 kcal mol(-1) and DeltaS = +38.9 cal mol(-1) K(-1) at 20 degrees C. The binding reaction is clearly entropically driven, a hallmark of a process that is predominantly stabilized by hydrophobic interactions, though a deeper analysis of the free energy contributions suggests that direct molecular recognition between echinomycin and DNA, mediated by hydrogen bonding and van der Waals contacts, also plays an important role in stabilizing the complex." @default.
• W2111332057 created "2016-06-24" @default.
• W2111332057 creator A5052764656 @default.
• W2111332057 creator A5063837282 @default.
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• W2111332057 date "2003-11-01" @default.
• W2111332057 modified "2023-10-16" @default.
• W2111332057 title "Energetics of echinomycin binding to DNA" @default.
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• W2111332057 doi "https://doi.org/10.1093/nar/gkg826" @default.
• W2111332057 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/275468" @default.
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• W2111332057 hasPublicationYear "2003" @default.
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