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Purification and NMR studies on Phosphatase domain of UBLCP1
이원태,신항철,Sunjin Moon,Sunggeon Ko,Hyosun Oh 한국자기공명학회 2009 Journal of the Korean Magnetic Resonance Society Vol.13 No.2
UBLCP1 is composed of Ubiquitin Like domain and RNA Polymerase Ⅱ PhosphataseⅠdomain. Phosphatase domain (25.9KDa) has been cloned into the E.coli using pET32a vector with TEV protease cleavage site and successfully purified as a monomer using affinity chromatography and histidine tag was cleaved with TEV protease for structural studies. Our results indicated that the Phosphatase domain showed well-defined folded structure based on data from one-dimensional and two-dimensional NMR spectroscopy. Data form circular dichroism also suggested that Phosphatase domain consisted of both α-helix and β-sheet. This information will be used for detailed structural study of UBLCP1.
Purification and Structural Studies on Human Pro-ghrelin
이원태,윤지혜,이지원 한국자기공명학회 2008 Journal of the Korean Magnetic Resonance Society Vol.12 No.1
Ghrelin is a unique peptide hormone that releases growth factor and it stimulates appetite. It comes from pre pro-ghrelin by the post translational modification process and its innate functions are known as food up-take and the growth hormone regulation. Therefore, the structural information of ghrelin precursor is of importance in understanding it function. From our results, we found that the solution structure of ghrelin is mostly random coil conformation at neutral pH value and the structural population changes with pH environments. Data from circular dichroism in different TFE concentrations revealed that the secondary structure changes from random coil to α-helix and the isodichroic point is observed at 202nm, implying that two equilibrium states exist between random coil and helical structure