eSPC: an online data-analysis platform for molecular biophysics
| Autor: | Lucas A. Defelipe, Christian M. Günther, Maria Marta Garcia Alai, Osvaldo Burastero, Stephan Niebling, Angelica Struve |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
K d
Kinetics eSPC online servers Ligands 01 natural sciences Online Systems Fluorescence spectroscopy Thermophoresis Fluorescence 03 medical and health sciences Structural Biology open science binding affinity molecular biophysics Cyclic GMP-Dependent Protein Kinases differential scanning fluorimetry T m 030304 developmental biology Binding affinities chemistry.chemical_classification 0303 health sciences ligand screening Microscale thermophoresis Biomolecule Molecular biophysics Temperature Mycobacterium tuberculosis microscale thermophoresis 0104 chemical sciences 010404 medicinal & biomolecular chemistry Spectrometry Fluorescence chemistry protein stability Thermodynamics Biological system Ccp4 molecular interactions Protein Binding |
| Zdroj: | Acta Crystallographica. Section D, Structural Biology |
| ISSN: | 2059-7983 |
| Popis: | eSPC is an online tool to analyze biophysical data from fluorescence, microscale thermophoresis and differential scanning fluorimetry experiments. The modules from the data-analysis platform contain classical thermodynamic models and clear user guidelines for the determination of dissociation constants (K d) and thermal unfolding parameters such as melting temperatures (T m). 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). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |