Isothermal Analysis of ThermoFluor Data can readily provide Quantitative Binding Affinities.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
25 02 2019
25 02 2019
Historique:
received:
23
07
2018
accepted:
30
11
2018
entrez:
27
2
2019
pubmed:
26
2
2019
medline:
20
9
2020
Statut:
epublish
Résumé
Differential scanning fluorimetry (DSF), also known as ThermoFluor or Thermal Shift Assay, has become a commonly-used approach for detecting protein-ligand interactions, particularly in the context of fragment screening. Upon binding to a folded protein, most ligands stabilize the protein; thus, observing an increase in the temperature at which the protein unfolds as a function of ligand concentration can serve as evidence of a direct interaction. While experimental protocols for this assay are well-developed, it is not straightforward to extract binding constants from the resulting data. Because of this, DSF is often used to probe for an interaction, but not to quantify the corresponding binding constant (K
Identifiants
pubmed: 30804351
doi: 10.1038/s41598-018-37072-x
pii: 10.1038/s41598-018-37072-x
pmc: PMC6389909
doi:
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2650Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM112736
Pays : United States
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