eSPC: an online data-analysis platform for molecular biophysics

All biological processes rely on the formation of protein-ligand, protein- peptide and protein-protein complexes. Studying the affinity, kinetics and thermodynamics of binding between these pairs is critical for understanding basic cellular mechanisms. Many different technologies have been designed for probing interactions between biomolecules, each based on measuring different signals (fluorescence, heat, thermophoresis, scattering and interference, among others). Evaluation of the data from binding experiments and their fitting is an essential step towards the quantification of binding affinities. Here, user-friendly online tools to analyze biophysical data from steady-state fluorescence spectroscopy, microscale thermophoresis and differential scanning fluorimetry experiments are presented. The modules of the data-analysis platform (https:// spc.embl-hamburg.de/) contain classical thermodynamic models and clear user guidelines for the determination of equilibrium dissociation constants (K-d) and thermal unfolding parameters such as melting temperatures (T-m).

Automated summary

The text discusses the importance of studying protein-ligand, protein-peptide, and protein-protein complexes in biological processes. Various technologies have been developed to probe interactions between biomolecules based on different signals such as fluorescence, heat, and scattering. Analysis and fitting of binding data are essential for quantifying binding affinities.