eSPC: An online data-analysis platform for molecular biophysics

Autores
Burastero, Osvaldo; Niebling, Stephan; Defelipe, Lucas Alfredo; Günther, Christian; Struve, Angelica; Garcia Alai, Maria M.
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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).
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
Fil: Niebling, Stephan. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Fil: Defelipe, Lucas Alfredo. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Günther, Christian. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Fil: Struve, Angelica. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Fil: Garcia Alai, Maria M.. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Materia
BINDING AFFINITY
DIFFERENTIAL SCANNING FLUORIMETRY
ESPC
KD
LIGAND SCREENING
MICROSCALE THERMOPHORESIS
MOLECULAR BIOPHYSICS
MOLECULAR INTERACTIONS
ONLINE SERVERS
OPEN SCIENCE
PROTEIN STABILITY
TM
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/210801
Acceder
id CONICETDig_f2716fd51bdf79e2d3df786ddfffef76
oai_identifier_str oai:ri.conicet.gov.ar:11336/210801
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling eSPC: An online data-analysis platform for molecular biophysicsBurastero, OsvaldoNiebling, StephanDefelipe, Lucas AlfredoGünther, ChristianStruve, AngelicaGarcia Alai, Maria M.BINDING AFFINITYDIFFERENTIAL SCANNING FLUORIMETRYESPCKDLIGAND SCREENINGMICROSCALE THERMOPHORESISMOLECULAR BIOPHYSICSMOLECULAR INTERACTIONSONLINE SERVERSOPEN SCIENCEPROTEIN STABILITYTMhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1All 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).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; ArgentinaFil: Niebling, Stephan. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; AlemaniaFil: Defelipe, Lucas Alfredo. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Günther, Christian. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; AlemaniaFil: Struve, Angelica. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; AlemaniaFil: Garcia Alai, Maria M.. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; AlemaniaInternational Union of Crystallography2021-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/210801Burastero, 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; 1241-12502059-7983CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://scripts.iucr.org/cgi-bin/paper?S2059798321008998info:eu-repo/semantics/altIdentifier/doi/10.1107/S2059798321008998info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:12:21Zoai:ri.conicet.gov.ar:11336/210801instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:12:21.995CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv eSPC: An online data-analysis platform for molecular biophysics
title eSPC: An online data-analysis platform for molecular biophysics
spellingShingle eSPC: An online data-analysis platform for molecular biophysics
Burastero, Osvaldo
BINDING AFFINITY
DIFFERENTIAL SCANNING FLUORIMETRY
ESPC
KD
LIGAND SCREENING
MICROSCALE THERMOPHORESIS
MOLECULAR BIOPHYSICS
MOLECULAR INTERACTIONS
ONLINE SERVERS
OPEN SCIENCE
PROTEIN STABILITY
TM
title_short eSPC: An online data-analysis platform for molecular biophysics
title_full eSPC: An online data-analysis platform for molecular biophysics
title_fullStr eSPC: An online data-analysis platform for molecular biophysics
title_full_unstemmed eSPC: An online data-analysis platform for molecular biophysics
title_sort eSPC: An online data-analysis platform for molecular biophysics
dc.creator.none.fl_str_mv Burastero, Osvaldo
Niebling, Stephan
Defelipe, Lucas Alfredo
Günther, Christian
Struve, Angelica
Garcia Alai, Maria M.
author Burastero, Osvaldo
author_facet Burastero, Osvaldo
Niebling, Stephan
Defelipe, Lucas Alfredo
Günther, Christian
Struve, Angelica
Garcia Alai, Maria M.
author_role author
author2 Niebling, Stephan
Defelipe, Lucas Alfredo
Günther, Christian
Struve, Angelica
Garcia Alai, Maria M.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv BINDING AFFINITY
DIFFERENTIAL SCANNING FLUORIMETRY
ESPC
KD
LIGAND SCREENING
MICROSCALE THERMOPHORESIS
MOLECULAR BIOPHYSICS
MOLECULAR INTERACTIONS
ONLINE SERVERS
OPEN SCIENCE
PROTEIN STABILITY
TM
topic BINDING AFFINITY
DIFFERENTIAL SCANNING FLUORIMETRY
ESPC
KD
LIGAND SCREENING
MICROSCALE THERMOPHORESIS
MOLECULAR BIOPHYSICS
MOLECULAR INTERACTIONS
ONLINE SERVERS
OPEN SCIENCE
PROTEIN STABILITY
TM
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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).
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
Fil: Niebling, Stephan. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Fil: Defelipe, Lucas Alfredo. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Günther, Christian. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Fil: Struve, Angelica. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
Fil: Garcia Alai, Maria M.. Centre For Structural Systems Biology; Alemania. European Molecular Biology Laboratory Hamburg; Alemania
description 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).
publishDate 2021
dc.date.none.fl_str_mv 2021-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/210801
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
2059-7983
CONICET Digital
CONICET
url http://hdl.handle.net/11336/210801
identifier_str_mv 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
2059-7983
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://scripts.iucr.org/cgi-bin/paper?S2059798321008998
info:eu-repo/semantics/altIdentifier/doi/10.1107/S2059798321008998
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv International Union of Crystallography
publisher.none.fl_str_mv International Union of Crystallography
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844614030193328128
score 13.070432

Publicaciones similares