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  2. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    This method use DNA recombinant technology and it gives an actual measurement of protein stability. In his detailed site-directed mutagenesis studies, Utani and his coworkers substituted 19 amino acids at Trp49 of the tryptophan synthase and he measured the free energy of unfolding.

  3. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [2] spectroscopic analytical procedure used to measure the concentration of protein in a solution. The reaction is dependent on the amino acid composition of the measured proteins.

  4. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    Size exclusion chromatography can be used directly to access protein stability in the presence or absence of ligands. [31] Samples of purified protein are heated in a water bath or thermocycler, cooled, centrifuged to remove aggregated proteins, and run on an analytical HPLC. As the melting temperature is reached and protein precipitates or ...

  5. 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]

  6. Instability index - Wikipedia

    en.wikipedia.org/wiki/Instability_Index

    The Instability index is a measure of proteins, used to determine whether it will be stable in a test tube. If the index is less than 40, then it is probably stable in the test tube. If it is greater (for example, enaptin ) then it is probably not stable.

  7. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.

  8. In situ cyclization of proteins - Wikipedia

    en.wikipedia.org/.../In_situ_cyclization_of_proteins

    The resulting crosslinked proteins or protein complexes have been shown to exhibit increased stability towards thermal and chemical stress and a lower tendency towards aggregation. [ 1 ] [ 6 ] So far, the melting temperature of proteins was increased by up to 39°C in a single design step.

  9. 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 ...