eSPC: an online data-analysis platform for molecular biophysics.
Acta Crystallogr D Struct Biol
; 77(Pt 10): 1241-1250, 2021 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-34605428
ABSTRACT
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 (Kd) and thermal unfolding parameters such as melting temperatures (Tm).
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1
Base de datos:
MEDLINE
Asunto principal:
Temperatura
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Termodinámica
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Sistemas en Línea
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Proteínas Quinasas Dependientes de GMP Cíclico
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Fluorescencia
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Mycobacterium tuberculosis
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Año:
2021
Tipo del documento:
Article