𝔖 Bobbio Scriptorium
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A Toolbox of GFP Technologies : Monitoring Protein Folding, Expression and Solubility

✍ Scribed by Stéphanie Cabantous; Thomas C. Terwilliger; Geoffrey S. Waldo; Jean-Denis Pédelacq

Book ID
102278188
Publisher
Wiley (John Wiley & Sons)
Year
2006
Weight
311 KB
Volume
8
Category
Article
ISSN
1439-4243

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✦ Synopsis

The green fluorescent protein (GFP) from the jellyfish Aequorea victoria is a single domain protein of 238 amino acids. The protein becomes highly fluorescent after it folds into its 3-dimensional structure and a post-translational autocatalytic cyclisation/dehydration of the tripeptide segment -S65-Y66-G67-occurs and creates a fluorophore.

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We have constructed three plasmid vectors for the expression of green fluorescent protein (GFP) fusion proteins using the following motif: (His) 6 -GFP-EK-X, where X represents chloramphenicol acetyl-transferase (CAT), human interleukin-2 (hIL-2), and organophosphorous hydrolase (OPH), respectively,