A rewired green fluorescent protein: Folding and function in a nonsequential, noncircular GFP permutant

Philippa J. Reeder, Yao Ming Huang, Jonathan S. Dordick, Christopher Bystroff

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The sequential order of secondary structural elements in proteins affects the folding and activity to an unknown extent. To test the dependence on sequential connectivity, we reconnected secondary structural elements by their solvent-exposed ends, permuting their sequential order, called "rewiring". This new protein design strategy changes the topology of the backbone without changing the core side chain packing arrangement. While circular and noncircular permutations have been observed in protein structures that are not related by sequence homology, to date no one has attempted to rationally design and construct a protein with a sequence that is noncircularly permuted while conserving three-dimensional structure. Herein, we show that green fluorescent protein can be rewired, still functionally fold, and exhibit wild-type fluorescence excitation and emission spectra.

Original languageEnglish
Pages (from-to)10773-10779
Number of pages7
JournalBiochemistry
Volume49
Issue number51
DOIs
StatePublished - 28 Dec 2010
Externally publishedYes

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