Synthetic Control of Green Fluorescent Protein

摘要

We recently demonstrated that semisynthetic green fluorescent protein (GFP) can be assembled by adding a synthetic peptide to a truncated protein that is produced recombinantly.This in vitro assembly mimics the in vivo assembly of "split GFP" used for protein solubility assays and protein colocalization. Unfortunately, recombinant expression of truncated GFPs often results in low sample yield5 with the chromophore either not formed or partially formed.Here we present a method that overcomes both of these limitations and enables efficient synthetic control of all residues, including those in the chro-mophore-containing interior a-helix.