Understanding the folding of GFP using biophysical techniques

Authors: Jackson, Sophie E; Craggs, Timothy D; Huang, Jie-rong

Source: Expert Review of Proteomics, Volume 3, Number 5, October 2006 , pp. 545-559(15)

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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.

Keywords: aggregation; denatured state; equilibrium intermediate; kinetic intermediate; misfolding; oligomeric state; protein folding selection

Document Type: Research article

DOI: http://dx.doi.org/10.1586/14789450.3.5.545

Affiliations: 1: Chemistry Department, Lensfield Road, Cambridge CB2 1EW, UK., Email: sej13@cam.ac.uk

Publication date: 2006-10-01

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Expert Review of Proteomics explores technologies, methods and discoveries from the field of proteomics to advance scientific understanding of the many varied roles protein expression plays in human health and disease.
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