Abstract
Abstract s-DL4 is a variant of green fluorescent protein (GFP), exclusively deposited in vivo into active inclusion bodies (IBs). In this study, we demonstrated that s-DL4 is a self-aggregating molecule by performing structural analysis of s-DL4 IBs and studying in vivo/in vitro aggregating properties of the molecule. Fourier transform infrared analysis of IBs revealed that there were native GFP structures and intermolecular interactions between the protein molecules. s-DL4 was always deposited into insoluble intracellular IB aggregates, regardless of the protein expression rate. The active s-DL4 IBs dissolved in urea solution were aggregated and precipitated when the urea was removed by dialysis.
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