Engineering and characterization of a superfolder green fluorescent protein

Article Abstract:

A robustly folded version of green fluorescent protein (GFP) that folds well even when fused to poorly folded polypeptides is generated and characterized. The results of characterization show that the fluorescence of superfolder GFP is unaffected by fusion partner misfolding and is directly proportional to total expression regardless of the solubility of the fusion, making superfolder GFP fluorescence a robust reporter of fusion protein expression.

Protein folding, Polypeptides, Protein research

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Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein

Article Abstract:

Several pairs of fragments from either the folding reporter green fluorescent protein (GFP), which contains the mutations F99S, MI53T, V163A, F64L and S65T or the exceptionally stable 'superfolder' GFP containing mutations S30R, Y39N, N105T, Y145F, I171V and A206V was tested to achieve the split GFP protein tagging and detection scheme. Findings revealed that the split GFP system is simple and does not change fusion protein solubility.

Proteins, Fluorescent chemicals

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Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies

Article Abstract:

Attempt is made to use alternative ligands to summarize the binding of antibodies, concentrating regions of diversity on one face of the protein. Selection of specific fluorobodies, its uses and properties are stated.

Usage, Influence, Viral antibodies, Antibodies, Properties, Binding proteins

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