Following the success of the human genome project, the need for efficient, economical production of genetically engineered proteins has emerged for both structural biology and the development of new biopharmaceuticals. Escherichia coli, as the first choice of host for the reason of speed and simplicity, still retains its dominant position. However massive, rapid expression of genetically engineered proteins in bacteria often results in the accumulation of the protein product in inactive insoluble deposits inside the cells, called “inclusion bodies”.
Formation of inclusion bodies has been the bottleneck for both biological research and commercial manufacture of biopharmaceuticals. Inclusion bodies are dense aggregates of misfolded polypeptide that can be found in both the cytoplasmic and periplasmic space of bacteria. Some proteins with native structure have integrated with inclusion bodies, but the quantity is usually minimal. Therefore protein must be released from the inclusion bodies followed by refolding to give its bioactivity and native 3D structure. This project is focusing on detecting the protein aggregation mechanism and getting a rapid and cost-efficient access to protein refolding.
Education:
1995-2000 Bachelor Degree of Science ChungChun University of Traditional Chinese Medicine, China
2000-2003 Master Degree of Science ChungChun University of Traditional Chinese Medicine, China
National Certified Doctor of China
Awards and Scholarships:
Australian Postgraduate Award 2005

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