What is the effect of higher hydrophobicity in proteins during purification?

Higher hydrophobicity in proteins during purification leads to the scenario where these proteins exhibit stronger interactions with hydrophobic surfaces, such as those found in affinity chromatography or other forms of column purification. When proteins have a higher degree of hydrophobicity, they can bind more tightly to the hydrophobic groups immobilized on the beads in the purification column.

This is primarily due to the nature of hydrophobic interactions, where nonpolar regions of the protein will associate more favorably with nonpolar surfaces, effectively enhancing the binding affinity. As a result, hydrophobic proteins tend to remain bound to the column longer and require stronger conditions or specific elution buffers to release them compared to less hydrophobic proteins. This principle is often utilized in techniques like hydrophobic interaction chromatography to separate proteins based on their hydrophobic characteristics.

Thus, when dealing with higher hydrophobicity in proteins during purification, it is expected that these proteins will stick tighter to the beads, facilitating their selective retention and later separation from other components in the mixture.