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Understanding the folding of GFP using biophysical techniques

Jackson, Sophie E. and Craggs, Timothy D. and Huang, Jie-rong. (2006) Understanding the folding of GFP using biophysical techniques. Expert review of proteomics, Vol. 3, H. 5. pp. 545-559.

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Official URL: http://edoc.unibas.ch/dok/A5249196

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Abstract

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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Grzesiek)
UniBasel Contributors:Huang, Jie-rong
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:22 Mar 2012 14:26
Deposited On:22 Mar 2012 13:49

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