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  2. Folding funnel - Wikipedia

    en.wikipedia.org/wiki/Folding_funnel

    The diagram sketches how proteins fold into their native structures by minimizing their free energy. The folding funnel hypothesis is a specific version of the energy landscape theory of protein folding, which assumes that a protein's native state corresponds to its free energy minimum under the solution conditions usually encountered in cells.

  3. 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.

  4. 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 ...

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  6. Hemodynamics - Wikipedia

    en.wikipedia.org/wiki/Hemodynamics

    For this reason, the blood flow velocity is the fastest in the middle of the vessel and slowest at the vessel wall. In most cases, the mean velocity is used. [18] There are many ways to measure blood flow velocity, like videocapillary microscoping with frame-to-frame analysis, or laser Doppler anemometry. [19]

  7. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    Figure 3. A salt bridge in T4 lysozyme between aspartic acid (Asp) at residue 70 and a histidine (His) at residue 31. The contribution of a salt bridge to the overall stability to the folded state of a protein can be assessed through thermodynamic data gathered from mutagenesis studies and nuclear magnetic resonance techniques. [13]

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

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

    800-290-4726 more ways to reach us. Sign in. Mail. 24/7 Help. For premium support please call: ... Do You Need to Increase Protein Intake As You Age? Jennifer Acker. February 7, 2024 at 11:45 AM.

  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 ...