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Quantitative in vivo solubility and reconstitution of truncated circular permutants of green fluorescent protein
Author(s) -
Huang YaoMing,
Nayak Sasmita,
Bystroff Christopher
Publication year - 2011
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.735
Subject(s) - green fluorescent protein , fluorescence , in vivo , fluorescent protein , solubility , chemistry , biophysics , circular dna , biology , biochemistry , gene , genetics , physics , organic chemistry , quantum mechanics , genome
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.