http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Keehyung Joo,Mi-Sun Kim,Jimin Park,Jooyoung Lee,Dong Hae Shin 한국구조생물학회 2015 Biodesign Vol.3 No.3
We have solved the crystal structures of predicted fructose-specific enzyme IIBfruc from Escherichia coli (EcEIIBfruc) and D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase from Burkholderia thailandensis (BtGmhB) of which the X-ray data contain various crystallographic problems. The bottleneck of the structural determination by X-ray crystallography was the phasing of the diffraction data. The obstacles were overcome by molecular replacement (MR) using the GOT(Global-Optimization-based Template-based modeling of proteins) models combined with the exhaustive search by bruteforce automation of phasing trials. This study suggests that the current computational approach can be applied to many unsolved MR problems where better 3D protein models are required or/and the MR solution is limited by the ambiguity in the crystallographic data.
Investigating Dynamics of Crowdfunding Policy (Extended Abstract)
Keehyung Kim 한국경영정보학회 2019 한국경영정보학회 학술대회논문집 Vol.2019 No.11
Crowdfunding has received a significant amount of attention from the public in the past few years. By lowering the entry barriers, crowdfunding platforms have allowed less-sophisticated investors to participate in an investment market. However, inexperienced crowd investors often lack ability and resources to correctly infer quality of various projects. When making an investment decision, they heavily rely on information provided by the project managers. To alleviate such information asymmetry between project managers and crowd investors, crowdfunding platforms have recently started to introduce a policy requiring project managers to disclose any potential risks involved in the project. This paper seeks to understand the role of risk disclosure policy in crowdfunding platforms and how it may affect the decisions of both project managers and crowd investors. We provide a model of crowdfunding and show how theoretical predictions of project quality and crowd investment differ across a number of disclosure policies. Based on the proposed model, we plan to employ laboratory economics experiments for empirical tests.
Crystal Structure of Hypothetical Fructose-Specific EIIB from Escherichia coli
Park, Jimin,Kim, Mi-Sun,Joo, Keehyung,Jhon, Gil-Ja,Berry, Edward A.,Lee, Jooyoung,Shin, Dong Hae Korean Society for Molecular and Cellular Biology 2016 Molecules and cells Vol.39 No.6
We have solved the crystal structure of a predicted fructose-specific enzyme $IIB^{fruc}$ from Escherichia coli ($EcEIIB^{fruc}$) involved in the phosphoenolpyruvate-carbohydrate phosphotransferase system transferring carbohydrates across the cytoplasmic membrane. $EcEIIB^{fruc}$ belongs to a sequence family with more than 5,000 sequence homologues with 25-99% amino-acid sequence identity. It reveals a conventional Rossmann-like ${\alpha}-{\beta}-{\alpha}$ sandwich fold with a unique ${\beta}$-sheet topology. Its C-terminus is longer than its closest relatives and forms an additional ${\beta}$-strand whereas the shorter C-terminus is random coil in the relatives. Interestingly, its core structure is similar to that of enzyme $IIB^{cellobiose}$ from E. coli ($EcIIB^{cel}$) transferring a phosphate moiety. In the active site of the closest $EcEIIB^{fruc}$ homologues, a unique motif CXXGXAHT comprising a P-loop like architecture including a histidine residue is found. The conserved cysteine on this loop may be deprotonated to act as a nucleophile similar to that of $EcIIB^{cel}$. The conserved histidine residue is presumed to bind the negatively charged phosphate. Therefore, we propose that the catalytic mechanism of $EcEIIB^{fruc}$ is similar to that of $EcIIB^{cel}$ transferring phosphoryl moiety to a specific carbohydrate.
Crystal Structure of Hypothetical Fructose-Specific EIIB from Escherichia coli
Dong Hae Shin,Jimin Park,김미선,Keehyung Joo,Gil-Ja Jhon,Edward A. Berry,Jooyoung Lee 한국분자세포생물학회 2016 Molecules and cells Vol.39 No.6
We have solved the crystal structure of a predicted fruc-tose-specific enzyme IIBfruc from Escherichia coli (EcEIIBfruc) involved in the phosphoenolpyruvate-carbohydrate phosphotransferase system transferring carbohydrates across the cytoplasmic membrane. EcEIIBfruc belongs to a sequence family with more than 5,000 sequence homologues with 25-99% amino-acid sequence identity. It reveals a conventional Rossmann-like -- sandwich fold with a unique -sheet topology. Its C-terminus is longer than its closest relatives and forms an additional -strand whereas the shorter C-terminus is random coil in the relatives. Interestingly, its core structure is similar to that of enzyme IIBcellobiose from E. coli (EcIIBcel) transferring a phosphate moiety. In the active site of the closest EcEIIBfruc homologues, a unique motif CXXGXAHT comprising a P-loop like architecture including a histidine residue is found. The conserved cysteine on this loop may be deprotonated to act as a nucleophile similar to that of EcIIBcel. The conserved histidine residue is presumed to bind the negatively charged phosphate. Therefore, we propose that the catalytic mechanism of EcEIIBfruc is similar to that of EcIIBcel transferring phosphoryl moiety to a specific carbohydrate.