Determination of free energy of double helix formation from two single-stranded polynucleotides and estimation of energetics of different low-molecular compounds binding to nucleic acids provide valuable tools for understanding of mechanisms that govern noncovalent binding of ligands to their receptor targets. In order to completely understand the molecular forces that drive and stabilize double helix formation and its complexes with ligands, thermodynamic studies are needed to complement the structural data. Structural characterization of a number of DNA-ligand complexes by X-ray and high-resolution NMR method provides key insight relating to the properties of complex formation, but structural data alone, even when coupled with the most sophisticated current computational methods, cannot fully define the driving forces for binding inte-ractions (or interac-tions) or even accurately predict their binding affinities. Thermodynamics provides quantitative data of use in elucidating these driving forces and for evaluating and understanding at a deeper level the effects of substituent changes on binding affinity.
Part of the book: Calorimetry