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  2. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    Proteins that have high hydrophobic amino acid content on the surface have low solubility in an aqueous solvent. Charged and polar surface residues interact with ionic groups in the solvent and increase the solubility of a protein. Knowledge of a protein's amino acid composition will aid in determining an ideal precipitation solvent and methods.

  3. Salting out - Wikipedia

    en.wikipedia.org/wiki/Salting_out

    Unwanted proteins can be removed from a protein solution mixture by salting out as long as the solubility of the protein in various concentrations of salt solution is known. After removing the precipitate by filtration or centrifugation , the desired protein can be precipitated by altering the salt concentration to the level at which the ...

  4. Immunoprecipitation - Wikipedia

    en.wikipedia.org/wiki/Immunoprecipitation

    Immunoprecipitation of intact protein complexes (i.e. antigen along with any proteins or ligands that are bound to it) is known as co-immunoprecipitation (Co-IP). Co-IP works by selecting an antibody that targets a known protein that is believed to be a member of a larger complex of proteins.

  5. Ammonium sulfate precipitation - Wikipedia

    en.wikipedia.org/wiki/Ammonium_sulfate_precipitation

    Ammonium sulfate precipitation is a useful technique as an initial step in protein purification because it enables quick, bulk precipitation of cellular proteins. [4] It is also often employed during the later stages of purification to concentrate protein from dilute solution following procedures such as gel filtration .

  6. Salt bridge (protein and supramolecular) - Wikipedia

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

    In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1). Ion pairing is one of the most important noncovalent forces in chemistry, in biological systems, in different materials and in many applications such as ion pair chromatography. It is a most commonly observed ...

  7. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    This could include bridging proteins, nucleic acids (DNA or RNA), or other molecules. Bimolecular fluorescence complementation (BiFC) is a new technique in observing the interactions of proteins. Combining with other new techniques, this method can be used to screen proteinprotein interactions and their modulators, [3] DERB. [4]

  8. Precipitation (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Precipitation_(chemistry)

    As proteins have complex tertiary and quaternary structures due to their specific folding and various weak intermolecular interactions (e.g., hydrogen bridges), these superstructures can be modified and proteins denaturated and precipitated. Another important application of an antisolvent is in ethanol precipitation of DNA.

  9. List of purification methods in chemistry - Wikipedia

    en.wikipedia.org/wiki/List_of_purification...

    Water purification combines a number of methods to produce potable or drinking water. Downstream processing refers to purification of chemicals, pharmaceuticals and food ingredients produced by fermentation or synthesized by plant and animal tissues, for example antibiotics , citric acid , vitamin E , and insulin .