ArticleJournal of biomolecular NMR2016
Optimization of protein samples for NMR using thermal shift assays.
Article in Journal of biomolecular NMR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- An NMR sample preparation case study: Considerations for the self-destructive protease caspase-6.PloS one · 2025Article
- Improving Stability ofBio-protocol · 2024Article
- The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.Science advances · 2024Article
- Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the ExtremophileMolecules (Basel, Switzerland) · 2024Article
- What's the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry.Methods (San Diego, Calif.) · 2023Review
- NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Screening of Buffers and Additives for Protein Stabilization by Thermal Shift Assay: A Practical Approach.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Methods for Structure Determination of SH2 Domain-Phosphopeptide Complexes by NMR.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Thermofluor-Based Optimization Strategy for the Stabilization of Recombinant Human Soluble Catechol-International journal of molecular sciences · 2022Article
- Experimental Investigation on the Bioprotective Role of Trehalose on Glutamine Solutions by Infrared Spectroscopy.Materials (Basel, Switzerland) · 2022Article
- Measuring Protein Aggregation and Stability Using High-Throughput Biophysical Approaches.Frontiers in molecular biosciences · 2022Article
- Thermofluor-Based Analysis of Protein Integrity and Ligand Interactions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structural insights into a HECT-type E3 ligase AREL1 and its ubiquitination activitiesThe Journal of biological chemistry · 2019Article
- Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic acids research · 2018Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maintaining a stable fold for recombinant proteins is challenging, especially when working with highly purified and concentrated samples at temperatures >20 °C. Therefore, it is worthwhile to screen for different buffer components that can stabilize protein samples. Thermal shift assays or ThermoFluor(®) provide a high-throughput screening method to assess the thermal stability of a sample under several conditions simultaneously. Here, we describe a thermal shift assay that is designed to optimize conditions for nuclear magnetic resonance studies, which typically require stable samples at high concentration and ambient (or higher) temperature. We demonstrate that for two challenging proteins, the multicomponent screen helped to identify ingredients that increased protein stability, leading to clear improvements in the quality of the spectra. Thermal shift assays provide an economic and time-efficient method to find optimal conditions for NMR structural studies.
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