eSPC

eSPC analyzes biophysical binding and stability data to quantify protein-ligand, protein-peptide, and protein-protein interactions and to extract thermodynamic parameters for molecular biophysics studies.

Key Features:

• Support for Multiple Technologies: Integrates steady-state fluorescence spectroscopy, microscale thermophoresis, and differential scanning fluorimetry and handles signals including fluorescence, heat, thermophoresis, scattering, and interference.
• Data Analysis Modules: Applies classical thermodynamic models to fit experimental binding and unfolding data.
• Quantification of Binding Affinities: Determines equilibrium dissociation constants (K_d) from binding experiments.
• Thermal Unfolding Parameters: Extracts melting temperatures (T_m) and other thermal unfolding parameters to assess protein stability and conformational changes.

Scientific Applications:

• Drug Discovery: Analysis of protein-ligand interactions to support selection of high-affinity ligands.
• Protein Engineering: Use of interaction and stability metrics to inform design of more stable or functional protein variants.
• Cellular Mechanism Elucidation: Quantification of protein-protein and protein-peptide interactions to investigate cellular pathways and mechanisms.

Methodology:

Experimental data are fitted to classical thermodynamic models to determine parameters such as K_d and T_m, using inputs from steady-state fluorescence spectroscopy, microscale thermophoresis, and differential scanning fluorimetry and accommodating signals of fluorescence, heat, thermophoresis, scattering, and interference.