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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. Proteostasis - Wikipedia

    en.wikipedia.org/wiki/Proteostasis

    Proteostasis is the dynamic regulation of a balanced, functional proteome.The proteostasis network includes competing and integrated biological pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell.

  4. Steady state (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Steady_state_(biochemistry)

    Steady-states can be stable or unstable. A steady-state is unstable if a small perturbation in one or more of the concentrations results in the system diverging from its state. In contrast, if a steady-state is stable, any perturbation will relax back to the original steady state. Further details can be found on the page Stability theory.

  5. Protein adsorption - Wikipedia

    en.wikipedia.org/wiki/Protein_adsorption

    In multi-protein system attraction between molecules can occur, whereas in single-protein solutions intermolecular repulsive interactions dominate. In addition, there is a time-dependent protein spreading, where protein molecules initially make contact with minimal binding sites on the surface.

  6. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Other factors suspected to affect degradation rate include the rate deamination of glutamine and asparagine and oxidation of cystein, histidine, and methionine, the absence of stabilizing ligands, the presence of attached carbohydrate or phosphate groups, the presence of free α-amino group, the negative charge of protein, and the flexibility ...

  8. Amino acid replacement - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_replacement

    Some amino acids are more likely to be replaced. One of the factors that influences this tendency is physicochemical distance. Example of a measure of amino acid can be Graur's Stability Index. [9] The assumption of this measure is that the amino acid replacement rate and protein's evolution is dependent on the amino acid composition of protein.

  9. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    Stability of beta barrel (β-barrel) transmembrane proteins is similar to stability of water-soluble proteins, based on chemical denaturation studies. Some of them are very stable even in chaotropic agents and high temperature. Their folding in vivo is facilitated by water-soluble chaperones, such as protein Skp. It is thought that β-barrel ...

  1. Related searches factors affecting protein stability and movement of molecules from one base

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