Work

Quantitative in vivo solubility and reconstitution of truncated circular permutants of green fluorescent protein

Year: 2011

Type: article

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.

Source: Protein Science

DOI: 10.1002/pro.735

Authors: Yao‐Ming Huang, Sasmita Nayak, Christopher Bystroff

Institution: Rensselaer Polytechnic Institute

Language: English

Topic: Advanced Fluorescence Microscopy Techniques

Subfield: Biophysics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Science Foundation, National Institutes of Health, National Institute of General Medical Sciences

Awards: Computational design of specific binding proteins using Leave-One-Out, Computational design of specific binding proteins using Leave-One-Out, Five Hierarchical Statistical Models for Protein Folding