Understanding the folding of GFP using biophysical techniques.
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.
Jackson
Sophie E
SE
Chemistry Department, Lensfield Road, Cambridge CB2 1EW, UK. sej13@cam.ac.uk
Craggs
Timothy D
TD
Huang
Jie-rong
JR
D049452:Green Fluorescent Proteins / Q000138:chemical synthesis / Q000737:chemistry*; D007700:Kinetics; D011489:Protein Denaturation; D015202:Protein Engineering / Q000379:methods; D017510:Protein Folding
D049452:Green Fluorescent Proteins