How does co-expression of chaperones influence GFP purification yield?

The co-expression of chaperones plays a significant role in the purification yield of GFP by improving its solubility and ensuring proper folding. Chaperones are proteins that assist in the correct folding and assembly of other proteins, helping to prevent misfolding and aggregation, which can occur when proteins are over-expressed in a cell.

By facilitating the correct conformational changes and preventing the formation of insoluble aggregates, chaperones increase the amount of correctly folded, functional GFP available during the purification process. This results in a higher yield of GFP that can be effectively purified and utilized for various applications, including research and biotechnology.

The other factors related to GFP, such as brightness, photostability, and protein aggregation, while important characteristics, do not directly correlate with the improvements in purification yield achieved through the action of chaperones. The focus of the question specifically asks about the influence on purification yield, making the enhancement of solubility and proper folding the most relevant factor.