Understanding the folding of GFP using biophysical techniques

Sophie E. Jackson*, Timothy D. Craggs, Jie Rong Huang

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

20 Scopus citations


Green fluorescent protein (GFP) and its many variants are probably the most widely used proteins in medical and biological research, having been extensively engineered to act as markers of gene expression and protein localization, indicators of protein-protein interactions and biosensors. GFP first folds, before it can undergo an autocatalytic cyclization and oxidation reaction to form the chromophore, and in many applications the folding efficiency of GFP is known to limit its use. Here, we review the recent literature on protein engineering studies that have improved the folding properties of GFP. In addition, we discuss in detail the biophysical work on the folding of GFP that is beginning to reveal how this large and complex structure forms.

Original languageEnglish
Pages (from-to)545-559
Number of pages15
JournalExpert Review of Proteomics
Issue number5
StatePublished - 2006


  • Aggregation
  • Denatured state
  • Equilibrium intermediate
  • Kinetic intermediate
  • Misfolding
  • Oligomeric state
  • Protein folding selection


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