The folding, stability and conformational dynamics of beta-barrel fluorescent proteins.
This critical review describes our current knowledge on the folding, stability and conformational dynamics of fluorescent proteins (FPs). The biophysical studies that have led to the elucidation of many of the key features of the complex energy landscape for folding for GFP and its variants are discussed. These illustrate some important issues surrounding how the large beta-barrel structure forms, and will be of interest to the protein folding community. In addition, the review highlights the importance of some of these results for the use of FPs in in vivo applications. The results should facilitate and aid in experimental designs of in vivo applications, as well as the interpretation of in vivo experimental data. The review is therefore of interest to all those working with FPs in vivo (103 references).
Hsu
Shang-Te Danny
ST
Chemistry Department, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW.
Blaser
Georg
G
Jackson
Sophie E
SE
D001703:Biophysics; D003198:Computer Simulation; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
D008565:Membrane Proteins; D049452:Green Fluorescent Proteins