FoldAffinity: Binding affinities from nDSF experiments

dc.creatorNiebling, Stephan
dc.creatorBurastero, Osvaldo
dc.creatorBürgi, Jérôme
dc.creatorGünther, Christian
dc.creatorDefelipe, Lucas Alfredo
dc.creatorSander, Simon
dc.creatorGattkowski, Ellen
dc.creatorAnjanappa, Raghavendra
dc.creatorWilmanns, Matthias
dc.creatorSpringer, Sebastian
dc.creatorTidow, Henning
dc.creatorGarcía Alai, María
dc.date2021-12
dc.date.accessioned2023-08-30T23:44:33Z
dc.date.available2023-08-30T23:44:33Z
dc.identifierhttp://hdl.handle.net/11336/182430
dc.identifierNiebling, Stephan; Burastero, Osvaldo; Bürgi, Jérôme; Günther, Christian; Defelipe, Lucas Alfredo; et al.; FoldAffinity: Binding affinities from nDSF experiments; Nature Publishing Group; Scientific Reports; 11; 1; 12-2021; 1-17
dc.identifier2045-2322
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8542734
dc.descriptionDifferential scanning fluorimetry (DSF) using the inherent fluorescence of proteins (nDSF) is a popular technique to evaluate thermal protein stability in different conditions (e.g. buffer, pH). In many cases, ligand binding increases thermal stability of a protein and often this can be detected as a clear shift in nDSF experiments. Here, we evaluate binding affinity quantification based on thermal shifts. We present four protein systems with different binding affinity ligands, ranging from nM to high μM. Our study suggests that binding affinities determined by isothermal analysis are in better agreement with those from established biophysical techniques (ITC and MST) compared to apparent Kds obtained from melting temperatures. In addition, we describe a method to optionally fit the heat capacity change upon unfolding (Δ Cp) during the isothermal analysis. This publication includes the release of a web server for easy and accessible application of isothermal analysis to nDSF data.
dc.descriptionFil: Niebling, Stephan. Centre for Structural Systems Biology; Alemania. European Molecular Biology Laboratory; Alemania
dc.descriptionFil: Burastero, Osvaldo. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. European Molecular Biology Laboratory; Alemania
dc.descriptionFil: Bürgi, Jérôme. European Molecular Biology Laboratory; Alemania
dc.descriptionFil: Günther, Christian. European Molecular Biology Laboratory; Alemania
dc.descriptionFil: Defelipe, Lucas Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. European Molecular Biology Laboratory; Alemania
dc.descriptionFil: Sander, Simon. Universitat Hamburg; Alemania
dc.descriptionFil: Gattkowski, Ellen. Universitat Hamburg; Alemania
dc.descriptionFil: Anjanappa, Raghavendra. Universitat Bremen. School of Engineering and Science Jacobs; Alemania
dc.descriptionFil: Wilmanns, Matthias. European Molecular Biology Laboratory; Alemania. Universitat Hamburg; Alemania
dc.descriptionFil: Springer, Sebastian. Universitat Bremen. School of Engineering and Science Jacobs; Alemania
dc.descriptionFil: Tidow, Henning. Universitat Hamburg; Alemania
dc.descriptionFil: García Alai, María. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania
dc.formatapplication/pdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherNature Publishing Group
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/s41598-021-88985-z
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-021-88985-z
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttps://creativecommons.org/licenses/by/2.5/ar/
dc.subjectNanoDSF
dc.subjectIsothermal Analysis
dc.subjectAffinity Determination
dc.subjecthttps://purl.org/becyt/ford/1.4
dc.subjecthttps://purl.org/becyt/ford/1
dc.titleFoldAffinity: Binding affinities from nDSF experiments
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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