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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. Heat shock response - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_response

    The heat shock response can be employed under stress to induce the expression of heat shock proteins (HSP), many of which are molecular chaperones, that help prevent or reverse protein misfolding and provide an environment for proper folding. [4] Protein folding is already challenging due to the crowded intracellular space where aberrant ...

  4. 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.

  5. Directed evolution - Wikipedia

    en.wikipedia.org/wiki/Directed_evolution

    Rational design of a protein relies on an in-depth knowledge of the protein structure, as well as its catalytic mechanism. [28] [29] Specific changes are then made by site-directed mutagenesis in an attempt to change the function of the protein. A drawback of this is that even when the structure and mechanism of action of the protein are well ...

  6. 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 ...

  7. 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 ...

  8. Do You Need to Increase Protein Intake As You Age? - AOL

    www.aol.com/increase-protein-intake-age...

    While researchers are still looking into why exactly we lose muscle as we age and the exact mechanisms behind decreased protein synthesis, Antonucci explains, research does show that increasing ...

  9. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    Calculating contacts is an important task in structural bioinformatics, being important for the correct prediction of protein structure and folding, thermodynamic stability, protein-protein and protein-ligand interactions, docking and molecular dynamics analyses, and so on. [8]