Characterization on the aggregation of self-aggregating green fluorescent protein variant

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• 作者：Govindan Raghunathan ; Ganapathiraman Munussami ; Sun-Gu Lee ; ^{sungulee@pusan.ac.kr}
• 关键词：Self-aggregation ; Protein-based particles ; Green fluorescent protein ; Inclusion bodies
• 刊名：Journal of Industrial and Engineering Chemistry
• 出版年：2017
• 出版时间：25 February 2017
• 年：2017
• 卷：46
• 期：Complete
• 页码：337-341
• 全文大小：784 K
• 卷排序：46

文摘

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.