In isoelectric precipitation, the protein will move along the gel in the certain pH until there is no electrostatic repulsion between molecules.

Solvent fractination is a separation method based on solubillity in inorganic solvent water.

The heat-unstable protein will remain in solution

If pH unit is above the pI value, it will have negative net charge. Therefore, anion exchange is used to bind the protein of interest.

In affinity chromatography, the matrix used MUST contain ligand so that it will specifically bind to a protein of interest.

The main purpose of SDS PAGE method is by positively charged the protein, so that it will migrate to the negative charge

In the amino acid analysis, ion exchange chromatography is a common method used to separate the amino acids in the sample.

PDCAAS is important because it estimates the protein nutritional quality based on weight gain divided by total protein consumed.

Emulsification is needed when there are a mixture of two or more immiscible liquids.

Proteins can be selectively precipitated or solubilized by changing buffer pH, ionic strength, dielectric constant, or temperature