What is a characteristic of hydrophobic interaction chromatography?

Hydrophobic interaction chromatography (HIC) is a technique specifically designed to separate molecules based on their hydrophobic properties. This method takes advantage of the varying degrees of hydrophobicity among different biomolecules, such as proteins, which allows for effective separation when a gradient of salt concentration is applied.

In HIC, hydrophobic regions of the molecules interact with the hydrophobic stationary phase of the column, facilitating the binding of more hydrophobic molecules while less hydrophobic ones are eluted first. As the salt concentration is gradually decreased, the bound hydrophobic molecules can be selectively eluted based on their affinity to the hydrophobic stationary phase. Thus, this method is crucial for purifying proteins and other biomolecules based on their hydrophobic characteristics.