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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. Nature's Fynd - Wikipedia

    en.wikipedia.org/wiki/Nature's_Fynd

    In March 2020, Sustainable Bioproducts rebranded as Nature's Fynd and closed an $80-million Series B round that enabled it to move into a 35,000-square-foot (3,300 m 2) plant in the Back of the Yards neighborhood near the old Union Stock Yard [4] to produce its geothermal springs-sourced microbe-based product, which has a more efficient ...

  5. 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 ...

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  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. ‘Blueprint Planet’ by Huffington Post

    testkitchen.huffingtonpost.com/blueprint

    Making a city "sustainable" means thinking about how to meet the housing, power, food and economic needs of its residents—not just today, but years from now. As a city's population swells, its leaders must plan ahead. They need to build resilience into communities that depend on government to deliver vital services.

  9. Depletion force - Wikipedia

    en.wikipedia.org/wiki/Depletion_force

    When the protein folds - this exclusion volume diminishes, making the folded state lower in free energy. Hence the excluded osmolytes shift the folding equilibrium towards the folded state. This effect was generally thought to be an entropic force, in the spirit of the original Asakura–Oosawa model and of macromolecular crowding .