Most of the biological phenomena are influenced by intermolecular recognition and interaction. Thus, understanding the thermodynamics of biomacromolecule ligand interaction is a very interesting area in biochemistry and biotechnology. One of the most powerful techniques to obtain precise information about the energetics of (bio) molecules binding to other biological macromolecules is isoth...

Effects of ?-cyclodextrin, ?CD, on refolding of lysozyme was investigated at pH 12 employing isothermal titration calorimetry (ITC) at 300K in 30mM Tris buffer solution. ?CD was employed as an anti-aggregation agent and the heats obtained for lysozyme+?CD interactions are reported and analyzed in terms of the extended solvation model. It was indicated that there are two sets of identical and no...

Detailed thermodynamic analysis of fragment binding revealed that unlike drug-like compounds, fragments bind with significant enthalpic preference. This observation is in line with the size dependency of binding enthalpy contributions and is also supported by a large body of experimental data from direct binding thermodynamic measurements. The enthalpy-driven binding of fragments represents a t...

A drug molecule should bind to its target with high affinity and selectivity. Because the binding affinity is a combined function of the binding enthalpy and the binding entropy, extremely high affinity requires that both terms contribute favorably to binding. The binding enthalpy, however, is notoriously more difficult to optimize than the binding entropy, a fact that has resulted in thermodyn...

The goal of this study is to use the model system described earlier to make direct measurements of the enthalpy of helix formation at different temperatures. For this we studied model alanine peptides in which helix formation can be triggered by metal (La(3+)) binding. The heat of La(3+) interaction with the peptides at different temperatures is measured by isothermal titration calorimetry. Cir...

A direct calorimetric measurement of the overall enthalpy change associated with self-assembly of organic monolayers at the liquid-solid interface is for most systems of interest practically impossible. In previous work we proposed an adapted Born-Haber cycle for an indirect assessment of the overall enthalpy change by using terephthalic acid monolayers at the nonanoic acid-graphite interface a...

Thermodynamic analysis provides access to the determinants of binding affinity, enthalpy and entropy. In fragment-based drug discovery (FBDD), thermodynamic analysis provides a powerful tool to discriminate fragments based on their potential for successful optimization. The thermodynamic data generated by FBDD studies can in turn be used to better understand the forces that drive biomolecular i...