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  2. 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]

  3. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    Using the above principles, equations that relate a global protein signal, corresponding to the folding states in equilibrium, and the variable value of a denaturing agent, either temperature or a chemical molecule, have been derived for homomeric and heteromeric proteins, from monomers to trimers and potentially tetramers.

  4. Protein aggregation - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation

    This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to shield themselves from the hydrophilic (water-loving) environment of the cell by burying into the interior of the protein. Thus, the exterior of a protein is typically hydrophilic, whereas the interior is typically ...

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein domains. The two shown protein structures share a common domain (maroon), the PH domain, which is involved in phosphatidylinositol (3,4,5)-trisphosphate binding. Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds.

  6. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    Biological proteins are made up of zwitterionic amino acid compounds; the net charge of these proteins can be positive or negative depending on the pH of the environment. The specific pI of the target protein can be used to model the process around and the compound can then be purified from the rest of the mixture.

  7. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...

  8. Salt bridge (protein and supramolecular) - Wikipedia

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

    [citation needed] In the T4 lysozyme example, ΔS of the pseudo-wild-type had previously been reported at pH 5.5 so the midpoint temperature difference of 11 °C at this pH multiplied by the reported ΔS of 360 cal/(mol·K) (1.5 kJ/(mol·K)) yields a free energy change of about −4 kcal/mol (−17 kJ/mol). This value corresponds to the amount ...

  9. Phi value analysis - Wikipedia

    en.wikipedia.org/wiki/Phi_value_analysis

    Phi value analysis assumes Hammond's postulate, which states that energy and chemical structure are correlated.Though the relationship between the folding intermediate and native state's structures may correlate that between their energies when the energy landscape has a well-defined, deep global minimum, free energy destabilizations may not give useful structural information when the energy ...