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  2. 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.

  3. Thermostability - Wikipedia

    en.wikipedia.org/wiki/Thermostability

    Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...

  4. Protein adsorption - Wikipedia

    en.wikipedia.org/wiki/Protein_adsorption

    Larger proteins are more likely to adsorb and remain attached to a surface due to the higher number of contact sites between amino acids and the surface (Figure 1). Figure 1. The effect of protein size on interaction with a surface. Notice that the larger protein composed of more amino acids is capable of making more interactions

  5. 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.

  6. The Best Protein Choices and Worst for Your Health and the ...

    www.aol.com/news/food-best-protein-choices-and...

    The Environmental Working Group (EWG, ewg.org) offers a "Meat Eaters Guide," which looks at the environmental impact of 20 The Best Protein Choices and Worst for Your Health and the Environment ...

  7. Directed evolution - Wikipedia

    en.wikipedia.org/wiki/Directed_evolution

    A drawback of this is that even when the structure and mechanism of action of the protein are well known, the change due to mutation is still difficult to predict. Therefore, an advantage of DE is that there is no need to understand the mechanism of the desired activity or how mutations would affect it.

  8. The Best Protein Choices and Worst for Your Health and the ...

    www.aol.com/lifestyle/food-best-protein-choices...

    The Environmental Working Group (EWG, ewg.org) offers a "Meat Eaters Guide," which looks at the environmental impact of 20 conventionally-grown protein sources, including beans, dairy, produce ...

  9. Macromolecular crowding - Wikipedia

    en.wikipedia.org/wiki/Macromolecular_crowding

    Due to macromolecular crowding, enzyme assays and biophysical measurements performed in dilute solution may fail to reflect the actual process and its kinetics taking place in the cytosol. [24] One approach to produce more accurate measurements would be to use highly concentrated extracts of cells, to try to maintain the cell contents in a more ...

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