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In the separation of proteins by hydrophobic interaction chromatography, why does eluent strength increase with decreasing salt concentration in the aqueous eluent?

Short Answer

Expert verified

Decreasing salt concentration increases protein solubility in aqueous mobile phase.

Step by step solution

01

Define hydrophobic interaction chromatography:

Hydrophobic interaction chromatography (HIC) classifies molecules based on their hydrophobicity.

02

Explanation for Hydrophobic interaction chromatography:

Hydrophobic interaction chromatography is a method used for separating molecules based on their hydrophobicity. The salt induces interactions between the hydrophobic and hydrophilic regions of the protein which promotes ligand - protein binding making the protein less soluble in mobile phase.

03

Decreasing salt concentration in the aqueous eluent:

Decreasing salt concentration increases protein solubility in aqueous mobile phase.

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