How can protein aggregation during purification be minimized?

Minimizing protein aggregation during purification is crucial to maintain the functionality and activity of proteins such as GFP. Optimizing temperature and ionic strength can significantly influence protein solubility and stability.

Maintaining an appropriate temperature is vital because proteins can become unstable at higher temperatures, which might lead to denaturation and aggregation. Similarly, ionic strength can affect protein interactions; too low ionic strength might lead to increased protein-protein interactions, whereas the right osmotic balance can promote solubility and keep proteins dispersed in solution.

By carefully controlling these parameters, one can create conditions that favor the correct folding and solubility of the protein while preventing misfolding and aggregation. This approach is supported by protein chemistry principles, where the environment around proteins can have profound effects on their behavior in solution during purification processes.

This understanding highlights how temperature and ionic strength adjustments can be effectively utilized to enhance purification outcomes and preserve the integrity of proteins.