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Circularly permuted variants of the green fluorescent protein.

S S Topell, J J Hennecke, and R R Glockshuber

FEBS Lett 457(2):283-9 (1999) PMID 10471794

Folding of the green fluorescent protein (GFP) from Aequorea victoria is characterized by autocatalytic formation of its p-hydroxybenzylideneimidazolidone chromophore, which is located in the center of an 11-stranded beta-barrel. We have analyzed the in vivo folding of 20 circularly permuted variants of GFP and find a relatively low tolerance towards disruption of the polypeptide chain by introduction of new termini. All permuted variants with termini in strands of the beta-barrel and about half of the variants with termini in loops lost the ability to form the chromophore. The thermal stability of the permuted GFPs with intact chromophore is very similar to that of the wild-type, indicating that chromophore-side chain interactions strongly contribute to the extraordinary stability of GFP.

Referenced by 1 articles

DOI: 10.1016/S0014-5793(99)01044-3
Version: za2963e q8za9 q8zb1 q8zc9 q8zd5 q8ze0 q8zfe q8zg5

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