Conflict of interest: CB has founded a company LOOP Biostructures LLC, with an interest in leave-one-out GFP.
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Quantitative in vivo solubility and reconstitution of truncated circular permutants of green fluorescent protein†
Article first published online: 5 OCT 2011
DOI: 10.1002/pro.735
Copyright © 2011 The Protein Society
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How to Cite
Huang, Y.-M., Nayak, S. and Bystroff, C. (2011), Quantitative in vivo solubility and reconstitution of truncated circular permutants of green fluorescent protein. Protein Science, 20: 1775–1780. doi: 10.1002/pro.735
- †
Publication History
- Issue published online: 18 OCT 2011
- Article first published online: 5 OCT 2011
- Accepted manuscript online: 9 SEP 2011 03:11PM EST
- Manuscript Accepted: 17 AUG 2011
- Manuscript Received: 26 APR 2011
Funded by
- National Science Foundation. Grant Number: DBI 0448072
- National Institutes of Health. Grant Number: GM88838
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Keywords:
- protein folding;
- leave-one-out;
- GFP;
- reconstitution;
- circular permutant
Abstract
Several versions of split green fluorescent protein (GFP) fold and reconstitute fluorescence, as do many circular permutants, but little is known about the dependence of reconstitution on circular permutation. Explored here is the capacity of GFP to fold and reconstitute fluorescence from various truncated circular permutants, herein called “leave-one-outs” using a quantitative in vivo solubility assay and in vivo reconstitution of fluorescence. Twelve leave-one-out permutants are discussed, one for each of the 12 secondary structure elements. The results expand the outlook for the use of permuted split GFPs as specific and self-reporting gene encoded affinity reagents.