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Issue 10, 2009
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Green fluorescent protein: structure, folding and chromophore maturation

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Abstract

The prolific use of green fluorescent protein and its variants throughout cellular biology relies on the post-translational formation of the chromophore, which proceeds without the need for any additional enzymes or cofactors, except molecular oxygen. In order to form the mature chromophore, the polypeptide backbone must undergo four distinct processes: folding, cyclisation, oxidation and dehydration. This tutorial review looks in detail at the proposed mechanisms for chromophore formation arising out of experimental and computational studies. The folding process is discussed, and the role that the native state plays in catalysing the initial cyclisation and subsequent chemistry is analysed. The specific functions of four conserved residues (Y66, G67, R96 and E222) in the maturation process are also presented. A greater understanding of the maturation process of fluorescent proteins from both jellyfish and coral species will profit the ongoing quest for brighter, faster maturing, genetically-encodable fluorescent probes of all colours, thus increasing their utility throughout the biomedical sciences.

Graphical abstract: Green fluorescent protein: structure, folding and chromophore maturation

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Publication details

The article was received on 29 Jun 2009 and first published on 26 Aug 2009


Article type: Tutorial Review
DOI: 10.1039/B903641P
Chem. Soc. Rev., 2009,38, 2865-2875

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    Green fluorescent protein: structure, folding and chromophore maturation

    T. D. Craggs, Chem. Soc. Rev., 2009, 38, 2865
    DOI: 10.1039/B903641P

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