At Creative Biostructure we offer several thermodynamics analytical services to study the binding mechanism of your biomolecules. The approach we use for binding or formulation analysis is to measure and identify the most stable interaction or conformation of the protein using a number of biophysical approaches. Characterizing and stabilizing the conformation of a molecule is key to developing a successful, stable, and robust formulation.
Measurements of binding thermodynamics extends the characterization of biomolecular interactions, since binding affinity is a function of two quantities: the enthalpy (ΔH) and entropy (ΔS). By exploiting binding thermodynamics the potential of enthalpy and entropy correlations associated with chemical modifications in different regions of the lead molecule can be specified enabling a more robust and reliable drug discovery process.
Figure 1. Thermodynamic view of protein association.
Creative Biostructure uses first-class instruments to analyze binding kinetics of a defined interaction between two biomolecules at a series of temperatures. Evaluation of interaction data obtained at varying temperatures provides van't Hoff and Eyring plots which yield thermodynamic constants for the equilibrium and transition state formation.
The facility provides real-time, label-free analysis for determination of thermodynamics of biomolecules, such as affinity, kinetics and concentration. Kinetic analysis including association and dissociation of biomolecules can be performed on up to 384 samples in one 384-well microplate.
Please contact our application specialists for getting detailed information and an individual quote. We also provide various protein analysis services to support your project.