The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.
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.
Institute for Biotechnology and Biomedicine, Department of Genetics and Microbiology, Autonomous University of Barcelona, Bellaterra, 08193 Barcelona, Spain.
Mónica
M
Martínez-Alonso
Nuria
N
González-Montalbán
Elena
E
García-Fruitós
Antonio
A
Villaverde
D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012995:Solubility
D011994:Recombinant Proteins; D049452:Green Fluorescent Proteins