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트립토판을 지닌 돌연변이 루신-대응 조절 단백질의 제조 및 분리
로버트포쿠 ( Robert Pokoo ),이의호 ( Euiho Lee ),권나희 ( Nahee Kwon ),이찬용 ( Chan Yong Lee ) 충남대학교 기초과학연구원 2022 충남과학연구지 Vol.39 No.1
Leucine-responsive regulatory protein (Lrp) is a global regulatory protein of molecular weight 18.8 kDa and is widely known to regulate a lot of metabolic and functional activities of operons in enteric bacteria such as Escherichia coli. This research study was designed with the aim of elucidating information about the mechanism by which Lrp protein is able to regulate the expression. In order to achieve this, mutant and wild type plasmids inserting the genes code for Lrp F57W, Lrp F90W, Lrp F93W, Lrp R145W, and Lrp Wt proteins were generated by site-directed mutagenesis and polymerase chain reaction. The tryptophan containing mutant Lrps which have intrinsic fluorescence characteristics obtained from this research experiments will give an information into the three dimensional structure of Lrp F57W, Lrp F90W, Lrp F93W, and Lrp R145W such as the orientation of the tryptophan as well as the distance between the binding site and tryptophan in the mutant proteins.