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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. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [1]

  4. Chevron plot - Wikipedia

    en.wikipedia.org/wiki/Chevron_plot

    A chevron plot is a way of representing protein folding kinetic data in the presence of varying concentrations of denaturant that disrupts the protein's native tertiary structure. The plot is known as "chevron" plot because of the canonical v , or chevron shape observed when the logarithm of the observed relaxation rate is plotted as a function ...

  5. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  6. Denaturation midpoint - Wikipedia

    en.wikipedia.org/wiki/Denaturation_midpoint

    Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.

  7. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    Using the above principles, equations that relate a global protein signal, corresponding to the folding states in equilibrium, and the variable value of a denaturing agent, either temperature or a chemical molecule, have been derived for homomeric and heteromeric proteins, from monomers to trimers and potentially tetramers.

  8. Precipitation (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Precipitation_(chemistry)

    An example would be the synthesis of Cr 3+ tetraphenylporphyrin chloride: water is added to the dimethylformamide (DMF) solution in which the reaction occurred, and the product precipitates. [10] Precipitation is useful in purifying many other products: e.g. , crude bmim -Cl is taken up in acetonitrile , and dropped into ethyl acetate , where ...

  9. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    Other interference may come from the buffer used when preparing the protein sample. A high concentration of buffer will cause an overestimated protein concentration due to depletion of free protons from the solution by conjugate base from the buffer. This will not be a problem if a low concentration of protein (subsequently the buffer) is used. [6]