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dc.contributor.author
Burastero, Osvaldo
dc.contributor.author
Niebling, Stephan
dc.contributor.author
Defelipe, Lucas Alfredo
dc.contributor.author
Günther, Christian
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Struve, Angelica
dc.contributor.author
Garcia Alai, Maria M.
dc.date.available
2023-09-07T11:51:27Z
dc.date.issued
2021-10
dc.identifier.citation
Burastero, Osvaldo; Niebling, Stephan; Defelipe, Lucas Alfredo; Günther, Christian; Struve, Angelica; et al.; eSPC: An online data-analysis platform for molecular biophysics; International Union of Crystallography; Acta Crystallographica Section D: Structural Biology; 77; 10-2021; 1241-1250
dc.identifier.issn
2059-7983
dc.identifier.uri
http://hdl.handle.net/11336/210801
dc.description.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).
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
International Union of Crystallography
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
BINDING AFFINITY
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DIFFERENTIAL SCANNING FLUORIMETRY
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ESPC
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KD
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LIGAND SCREENING
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MICROSCALE THERMOPHORESIS
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MOLECULAR BIOPHYSICS
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MOLECULAR INTERACTIONS
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ONLINE SERVERS
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OPEN SCIENCE
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PROTEIN STABILITY
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TM
dc.subject.classification
Biofísica
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
eSPC: An online data-analysis platform for molecular biophysics
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-08-30T10:39:08Z
dc.journal.volume
77
dc.journal.pagination
1241-1250
dc.journal.pais
Reino Unido
dc.description.fil
Fil: Burastero, Osvaldo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Niebling, Stephan. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
dc.description.fil
Fil: Defelipe, Lucas Alfredo. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Günther, Christian. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
dc.description.fil
Fil: Struve, Angelica. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
dc.description.fil
Fil: Garcia Alai, Maria M.. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
dc.journal.title
Acta Crystallographica Section D: Structural Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://scripts.iucr.org/cgi-bin/paper?S2059798321008998
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1107/S2059798321008998
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