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  2. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...

  3. Cellular thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Cellular_thermal_shift_assay

    CEllular Thermal Shift Assay (CETSA ®) is a patented label free chemoproteomics method that has enabled measurements of compound target engagement in intact cells and tissue, without modifications to the target protein. This is accomplished by comparing the measured cellular thermal stability of the protein in the presence and absence of the ...

  4. Chemoproteomics - Wikipedia

    en.wikipedia.org/wiki/Chemoproteomics

    In a typical assay setup, protein-containing samples are exposed to a ligand of choice, then those samples are aliquoted and heated to separate individual temperature points. Upon binding to a ligand, a protein's thermal stability is expected to increase

  5. Nano differential scanning fluorimetry - Wikipedia

    en.wikipedia.org/wiki/Nano_differential_scanning...

    A nanoDSF assay is also known as a type of Thermal Shift Assay. Protein stability is typically addressed by thermal or chemical unfolding experiments. [2] In thermal unfolding experiments, a linear temperature ramp is applied to unfold proteins, whereas chemical unfolding experiments use chemical denaturants in increasing concentrations.

  6. Fast parallel proteolysis - Wikipedia

    en.wikipedia.org/wiki/Fast_parallel_proteolysis

    A protein mixture is aliquoted into several tubes, which are exposed in parallel to different temperatures and a thermostable protease. The remaining protein can be resolved on SDS-PAGE . Fast parallel proteolysis ( FASTpp ) is a method to determine the thermostability of proteins by measuring which fraction of protein resists rapid proteolytic ...

  7. Microscale thermophoresis - Wikipedia

    en.wikipedia.org/wiki/Microscale_thermophoresis

    The thermal relaxation induces a binding-dependent drop in the fluorescence of the dye due to its local environmental-dependent response to the temperature jump (TRIC). At the same time molecules typically move from the locally heated region to the outer cold regions.

  8. Lysozyme PEGylation - Wikipedia

    en.wikipedia.org/wiki/Lysozyme_PEGylation

    Lysozyme PEGylation is the covalent attachment of Polyethylene glycol (PEG) to Lysozyme, which is one of the most widely investigated PEGylated proteins.. The PEGylation of proteins has become a common practice of modern therapeutic drugs, as the process is capable of enhancing solubility, thermal stability, enzymatic degradation resistance, and serum half-life of the proteins of interest.

  9. Cycloheximide chase - Wikipedia

    en.wikipedia.org/wiki/Cycloheximide_chase

    Cycloheximide chase assays are an experimental technique used in molecular and cellular biology to measure steady state protein stability. Cycloheximide is a drug that inhibits the elongation step in eukaryotic protein translation, thereby preventing protein synthesis. [1]

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