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Protein precipitation refers to the concentration of proteins by altering their solubility to remove them from solution. Proteins are most often precipitated in three ways: 1) the addition of salt, 2) the addition of organic solvent, or 3) altering pH. The addition of salt causes the charged proteins to interacted with the salt instead of the the water and the protein falls out of solution. This process, called “salting out”, is the most common precipitation method and usually allows proteins to maintain their native structure. Organic solvent addition decreases the dielectric constant and encourages protein aggregation leading to precipitation. As with salting out, proteins can retain their native structure through this process. Precipitating by pH involves changing the pH of the solution to a point where the net charge of the protein to be precipitated is zero (isoelectric point). At a charge of zero the proteins will aggregate and precipitate. Precipitation by pH causes irreversible denaturation (unfolding) of the protein. This technique is commonly used to remove contaminants. In addition to the three most common methods, non-ionic polymer or metal ion addition can be used to precipitate proteins. Considerations when selecting a method include the importance of retaining the native structure and the purity desired. Precipitation is necessary for most protein purification protocols and is essential for protein crystallization. Precipitation is common in industrial manufacturing of protein-based drugs as well. (Credit: Brooke Anderson-White)
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