ArticleEuropean biophysics journal : EBJ2021
Standard operating procedure for fluorescent thermal shift assay (FTSA) for determination of protein-ligand binding and protein stability.
Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Protein Engineering and Drug Discovery: Importance, Methodologies, Challenges, and Prospects.Biomolecules · 2025Review
- Affinity and Selectivity of Protein-Ligand Recognition: A Minor Chemical Modification Changes Carbonic Anhydrase Binding Profile.Journal of medicinal chemistry · 2025Article
- Unlocking GPCR-ligand interactions: Measuring binding affinities with thermal shift assay.Protein science : a publication of the Protein Society · 2025Article
- Characterization of VldE (Spr1875), a Pneumococcal Two-State l,d-Endopeptidase with a Four-Zinc Cluster in the Active Site.ACS catalysis · 2024Article
- Chemoproteomics enables identification of coatomer subunit zeta-1 targeted by a small molecule for enterovirus A71 inhibition.MedComm · 2024Article
- Viral Receptor-Binding Protein Evolves New Function through Mutations That Cause Trimer Instability and Functional Heterogeneity.Molecular biology and evolution · 2024Article
- Application of particle swarm optimization to understand the mechanism of action of allosteric inhibitors of the enzyme HSD17β13.Patterns (New York, N.Y.) · 2023Article
- Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.International journal of molecular sciences · 2021Article
- Community-building and promotion of technological excellence in molecular biophysics: the ARBRE-MOBIEU network.European biophysics journal : EBJ · 2021Article
- Thiazide and other Cl-benzenesulfonamide-bearing clinical drug affinities for human carbonic anhydrases.PloS one · 2021Article
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Abstract
A standard operating procedure for a fluorescence-based thermal shift assay (FTSA) is provided describing its typical applications, advantages and limitations. FTSA is a simple, robust, universal and quick assay to determine protein-ligand binding affinities and protein stabilities in the presence of various excipients and solution conditions. Therefore, the assay is very useful for the straightforward characterization of new recombinantly produced proteins. The assay has a wide dynamic range enabling simultaneous determination of affinities in the milimolar to picomolar range. The assay could be used for essentially any protein that is sufficiently soluble and stable in the studied aqueous solution. Here we provide examples and typical experimental protocols for both affinity and stability determinations.
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