Which characteristic of GFP makes it particularly suitable for purification?

Green Fluorescent Protein (GFP) is particularly suitable for purification due to its abundance of hydrophobic amino acids. These hydrophobic regions promote strong interactions with certain types of chromatography media, such as hydrophobic interaction chromatography (HIC). During the purification process, these interactions can be effectively utilized to separate GFP from other proteins and contaminants in a mixture. The hydrophobic areas of GFP enable it to bind to the hydrophobic support in the column while less hydrophobic proteins will not bind as strongly or at all, allowing for a more efficient purification process.

The hydrophobic properties of GFP not only facilitate its binding to specific matrices but also help in stabilizing its structure, which is crucial for maintaining its fluorescent properties throughout the purification process. This characteristic of having many hydrophobic amino acids directly influences its behavior during purification, making it easier to isolate from a complex mixture of other proteins.