I am designing a bacterial protein interaction and co-localisation study
involving two interacting proteins.

One protein is very small (~7–8 kDa), while the other is approximately
25–30 kDa. Previous biochemical experiments (crystal structure and binding
studies) have confirmed that the two proteins interact, and one protein
modulates the function of the other.

My initial plan was to generate fluorescent protein fusions (EGFP and
mCherry) for live-cell co-localisation. However, I am concerned that fusing
a ~27–29 kDa fluorescent protein to the smaller protein may interfere with
its folding, localisation, or interaction.

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