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  2. Dithiothreitol - Wikipedia

    en.wikipedia.org/wiki/Dithiothreitol

    DTT is frequently used to reduce the disulfide bonds of proteins and, more generally, to prevent intramolecular and intermolecular disulfide bonds from forming between cysteine residues of proteins. However, even DTT cannot reduce buried (solvent-inaccessible) disulfide bonds, so reduction of disulfide bonds is sometimes carried out under ...

  3. TCEP - Wikipedia

    en.wikipedia.org/wiki/TCEP

    TCEP is often used as a reducing agent to break disulfide bonds within and between proteins as a preparatory step for gel electrophoresis.. Compared to the other two most common agents used for this purpose (dithiothreitol and β-mercaptoethanol), TCEP has the advantages of being odorless, a more powerful reducing agent, an irreversible reducing agent (in the sense that TCEP does not ...

  4. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    The native form of a protein is usually a single disulfide species, although some proteins may cycle between a few disulfide states as part of their function, e.g., thioredoxin. In proteins with more than two cysteines, non-native disulfide species may be formed, which are almost always misfolded.

  5. mTOR - Wikipedia

    en.wikipedia.org/wiki/MTOR

    The mammalian target of rapamycin (mTOR), [5] also referred to as the mechanistic target of rapamycin, and sometimes called FK506-binding protein 12-rapamycin-associated protein 1 (FRAP1), is a kinase that in humans is encoded by the MTOR gene. [6] [7] [8] mTOR is a member of the phosphatidylinositol 3-kinase-related kinase family of protein ...

  6. Substrate inhibition in bioreactors - Wikipedia

    en.wikipedia.org/wiki/Substrate_inhibition_in...

    Substrate inhibition in bioreactors occurs when the concentration of substrate (such as glucose, salts, or phenols [1]) exceeds the optimal parameters and reduces the growth rate of the cells within the bioreactor. This is often confused with substrate limitation, which describes environments in which cell growth is limited due to of low substrate.

  7. Protein production - Wikipedia

    en.wikipedia.org/wiki/Protein_production

    Protein production is the biotechnological process of generating a specific protein. It is typically achieved by the manipulation of gene expression in an organism such that it expresses large amounts of a recombinant gene .

  8. Protein crystallization - Wikipedia

    en.wikipedia.org/wiki/Protein_crystallization

    Initially, the droplet of protein solution contains comparatively low precipitant and protein concentrations, but as the drop and reservoir equilibrate, the precipitant and protein concentrations increase in the drop. If the appropriate crystallization solutions are used for a given protein, crystal growth occurs in the drop.

  9. Protein purification - Wikipedia

    en.wikipedia.org/wiki/Protein_purification

    The protein manufacturing cost remains high and there is a growing demand to develop cost efficient and rapid protein purification methods. Understanding of the different protein purification methods and optimizing the downstream processing are critical to minimize production costs while maintaining the quality of acceptable standards of homogeneity. [2]