Effects of rigidity of linker peptides on fusion protein function
Introduction Fusion protein technique has become an important tool for both biotechnology research and applications. The fusion of two or more proteins can facilitate the purification of proteins, make the proteins visible and rapidly quantitative, or confer other desired functions to the target proteins, thereby reducing the whole bioprocess cost of protein production, separation/purification and biocatalysis. While it has been proved to be a powerful technique, there are many problems in constructing the so called multifunctional fusion proteins, which need to be solved. For example, the functional domains fused together by genetic engineering may end up with weakened function or loss of the function during the protein expression. It has been implied that this problem resulted from the improper folding or limited flexibility of the protein domains linked together.
Chong Zhang Fengchun Ye Xin-Hui Xing
Institute of Biochemical Engineering,Department of Chemical Engineering,Tsinghua University,Beijing 100084,China
国际会议
The Eleventh China-Japan-Korea Joint Symposium on Enzyme Engineering(第十一届中日韩酶工程学术研讨会)
成都
英文
64-65
2010-11-05（万方平台首次上网日期，不代表论文的发表时间）