Optimization of protein samples for NMR using thermal shift assays
Optimization of protein samples for NMR using thermal shift assays
Abstract
Maintaining a stable fold for recombinant proteins is challenging, especially when working with highly purified and concentrated samples at temperatures >20Â*°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...
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03-22-2016 01:46 PM
[NMR paper] Optimization of protein samples for NMR using thermal shift assays.
Optimization of protein samples for NMR using thermal shift assays.
Optimization of protein samples for NMR using thermal shift assays.
J Biomol NMR. 2016 Mar 17;
Authors: Kozak S, Lercher L, Karanth MN, Meijers R, Carlomagno T, Boivin S
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...
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03-18-2016 05:23 PM
Increasing Throughput in Protein Thermal Shift Assays - Genetic Engineering & Biotechnology News
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Increasing Throughput in Protein Thermal Shift Assays
Genetic Engineering & Biotechnology News
Historically, protein interaction studies have been measured using an array of techniques, including nuclear magnetic resonance, differential scanning calorimetry, and surface plasma resonance imaging. Additionally, protein melt screening methods used ...
Increasing Throughput in Protein Thermal Shift Assays - Genetic Engineering & Biotechnology News
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[NMR paper] Metabolic changes during cellular senescence investigated by proton NMR-spectroscopy.
Metabolic changes during cellular senescence investigated by proton NMR-spectroscopy.
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Abstract
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Elucidating metabolic pathways for amino acid incorporation into dragline spider silk using 13C enrichment and solid state NMR.
Elucidating metabolic pathways for amino acid incorporation into dragline spider silk using 13C enrichment and solid state NMR.
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Abstract
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NMR and protein folding: equilibrium and stopped-flow studies.
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