eSPC: an online data-analysis platform for molecular biophysics.
Osvaldo Burastero, Stephan Niebling, Lucas A Defelipe, Christian Günther, Angelica Struve, Maria M Garcia Alai
Author Information
Osvaldo Burastero: Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Intendente Güiraldes 2620, Ciudad Autónoma de Buenos Aires, Argentina. ORCID
Stephan Niebling: European Molecular Biology Laboratory, EMBL Hamburg, Notkestrasse 85, 22607 Hamburg, Germany. ORCID
Lucas A Defelipe: European Molecular Biology Laboratory, EMBL Hamburg, Notkestrasse 85, 22607 Hamburg, Germany. ORCID
Christian Günther: European Molecular Biology Laboratory, EMBL Hamburg, Notkestrasse 85, 22607 Hamburg, Germany. ORCID
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) and thermal unfolding parameters such as melting temperatures (T).
