Proteins are typically denatured in such solvents and bind due to the hydrophobic nature of the entire polypeptide sequence. Since the majority of hydrophobic groups are located in the core of globular proteins, the binding is related to the denaturation of the protein and the accessibility of these groups to the column functional groups. Hydration of resin 2. Decanting fines 3. Equilibrating the resin and preparing a slurry 4.
Resins come either dry or preswollen.
If they are dry they need to be hydrated. The settled resin is therefore carefully decanted to discard these fines. The resin is then equilibrated in the buffer to be used for the analysis. Equilibration usually involves pH'ing the resin, or buffer exchanges. Finally, the slurry is degassed prior to packing the column.