Our group is interested in the quantitative biophysical analysis of drug-protein and protein-protein interactions at the molecular level. Biophysical methods are uniquely suited to study the thermodynamics and kinetics of interactions between macromolecules. In our group various biophysical techniques are available to characterize binding and assembly of macromolecules in solution, including fluorescence spectroscopy, UV spectroscopy, stopped-flow kinetics and circular dichroism. These methods can provide the accurate quantitative information about the binding affinity between macromolecules such as proteins and nucleic acids and small molecules. They also allow us to explore the interaction on the molecular level and obtain parameters such as the order of the binding kinetics, the kinetic rate constants and the thermodynamics of the interactions.
- Protein-protein interactions: to study the interaction between macromolecules involved in
- Drug-protein interactions: - Drugs used in fibrosis cystic therapy and mucin.
- Photosensitizer used in photodynamic therapy and plasma proteins like HSA and BSA
- PNA-DNA interactions: to study from a kinetic point of view this kind of interaction using the stopped flow technique.
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