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  2. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    Thermostable proteins are often more useful than their non-thermostable counterparts, e.g., DNA polymerase in the polymerase chain reaction, [7] so protein engineering often includes adding mutations to increase thermal stability. Protein crystallization is more successful for proteins with a higher melting point [8] and adding buffer ...

  3. 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.

  4. 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 ...

  5. Cycloheximide chase - Wikipedia

    en.wikipedia.org/wiki/Cycloheximide_chase

    Cycloheximide chases are also valuable for assessing how different mutations affect the stability of a protein. Experiments have been conducted in yeast and mammalian cells to determine the critical residues required for protein stability and how disease-associated mutations may be affecting protein half-lives within the cell.

  6. Chemoproteomics - Wikipedia

    en.wikipedia.org/wiki/Chemoproteomics

    Binding of a drug to a protein often leads to ligand-induced stabilization of the protein (1), which can be measured by comparing the amount of non-denatured protein remaining in a drug-treated sample to an untreated control. The change in protein stability can be visualized as a rightward shift in its stability curve (2).

  7. Gary J. Pielak - Wikipedia

    en.wikipedia.org/wiki/Gary_J._Pielak

    Gary J. Pielak (born July 17, 1955) is an American biological chemist who is known for developing quantitative techniques for measuring protein structure, stability, diffusion, and concentration in living cells, and under crowded conditions.

  8. Your Call: When do you gamble on a fake punt? - AOL

    www.aol.com/sports/call-gamble-fake-punt...

    And that wouldn’t even be Cousins’ last interception on the day! Neither team would score again, and the 17-13 total held up. Harbaugh escaped with the win, but against a more accurate team ...

  9. FoldX - Wikipedia

    en.wikipedia.org/wiki/FoldX

    For protein-protein interactions, or protein-DNA interactions FoldX calculates ∆∆G of interaction : ∆∆G ab = ∆G ab - (∆G a + ∆G b ) + ∆G kon + ∆S sc ∆G kon reflects the effect of electrostatic interactions on the k on . ∆S sc is the loss of translational and rotational entropy upon making the complex.