The Functional Quality of Soluble Recombinant Polypeptides Produced in <i>Escherichia coli</i> Is Defined by a Wide Conformational Spectrum

Abstract

We have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by the prevalence of a canonical native structure.