Article

The folding, stability and conformational dynamics of beta-barrel fluorescent proteins.

Chemistry Department, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW.
Chemical Society Reviews (impact factor: 28.76). 10/2009; 38(10):2951-65. DOI:10.1039/b908170b
Source: PubMed

ABSTRACT 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).

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Keywords

103 references
 
biophysical studies
 
complex energy landscape
 
conformational dynamics
 
current knowledge
 
experimental designs
 
fluorescent proteins
 
GFP
 
key features
 
large beta-barrel structure forms
 
protein folding community
 
vivo
 
vivo applications
 
vivo experimental data