Pub Date : 2016-12-20DOI: 10.6564/JKMRS.2016.20.4.109
S. Park, A. Lim
{"title":"113Cd and133Cs NMR Study of Nucleus-Phonon Interactions in Linear-Chain Perovskite-Type CsCdBr3","authors":"S. Park, A. Lim","doi":"10.6564/JKMRS.2016.20.4.109","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.4.109","url":null,"abstract":"","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"109-113"},"PeriodicalIF":0.3,"publicationDate":"2016-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329944","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-12-20DOI: 10.6564/JKMRS.2016.20.4.121
Dahye Yoon, Seohee Ma, Hyeonsoo Choi, H. Noh, Youngjun Ok, Suhkmann Kim
Bean sprouts are often cultivated in the circumstances prevailing in the improper using of germicide and growth enhancer. The influence of ingestion those bean sprouts are unknown. The components of the bean sprouts are needed to evaluate for food safety. The extracts of the control, 0.5 g/L germicide, 1 g/L germicide, 12.5 mL/L growth enhancer and 25 mL/L growth enhancer were used to compare the components in the experiment. the germicide and growth enhancer has substantially potential to influence the growth of the bean sprouts.
{"title":"Investigation of Germicide and Growth Enhancer Effects on Bean Sprout using NMR-based Metabolomics","authors":"Dahye Yoon, Seohee Ma, Hyeonsoo Choi, H. Noh, Youngjun Ok, Suhkmann Kim","doi":"10.6564/JKMRS.2016.20.4.121","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.4.121","url":null,"abstract":"Bean sprouts are often cultivated in the circumstances prevailing in the improper using of germicide and growth enhancer. The influence of ingestion those bean sprouts are unknown. The components of the bean sprouts are needed to evaluate for food safety. The extracts of the control, 0.5 g/L germicide, 1 g/L germicide, 12.5 mL/L growth enhancer and 25 mL/L growth enhancer were used to compare the components in the experiment. the germicide and growth enhancer has substantially potential to influence the growth of the bean sprouts.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"121-128"},"PeriodicalIF":0.3,"publicationDate":"2016-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-12-20DOI: 10.6564/JKMRS.2016.20.4.129
Sung-Sub Choi, Ji-sun Kim, Ji-ho Jeong, Yongae Kim
Transmembrane(TM) proteins are closely related to transport, channel formation, signaling, cell to cell interaction, so they are the crucial target of modern medicinal drugs. In order to study the structure and function of these TM proteins, it is important to prepare reasonable amounts of proteins. However, their preparation is seriously difficult and time-consuming due to insufficient yields and low solubility of TM proteins. We tried to produce large amounts of Syndecan-4 containing TM domain(SDC4-TM) that is related to the wound healing and tumor. Also, mutated SDC4-TM was studied to investigate structural change by modification of dimerization motif. We performed the structure determination by the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on N-H 2D SAMPI-4 solid-state NMR of SDC4-TM and computational modeling using Discovery Studio 2016.
跨膜蛋白与转运、通道形成、信号传导、细胞间相互作用密切相关，是现代药物的重要靶点。为了研究这些TM蛋白的结构和功能，制备适量的蛋白是非常重要的。然而，由于TM蛋白的产率不足和溶解度低，它们的制备非常困难和耗时。我们尝试大量生产含有TM结构域的Syndecan-4 (SDC4-TM)，该结构域与伤口愈合和肿瘤有关。此外，我们还研究了突变SDC4-TM通过修饰二聚化基序来观察其结构变化。我们基于SDC4-TM的N-H 2D SAMPI-4固态核磁共振和Discovery Studio 2016的计算建模，通过极性指数斜角(PISA)车轮模式分析来确定结构。
{"title":"Structural Change in Transmembrane Region of Syndecan-4 by Mutation","authors":"Sung-Sub Choi, Ji-sun Kim, Ji-ho Jeong, Yongae Kim","doi":"10.6564/JKMRS.2016.20.4.129","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.4.129","url":null,"abstract":"Transmembrane(TM) proteins are closely related to transport, channel formation, signaling, cell to cell interaction, so they are the crucial target of modern medicinal drugs. In order to study the structure and function of these TM proteins, it is important to prepare reasonable amounts of proteins. However, their preparation is seriously difficult and time-consuming due to insufficient yields and low solubility of TM proteins. We tried to produce large amounts of Syndecan-4 containing TM domain(SDC4-TM) that is related to the wound healing and tumor. Also, mutated SDC4-TM was studied to investigate structural change by modification of dimerization motif. We performed the structure determination by the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on N-H 2D SAMPI-4 solid-state NMR of SDC4-TM and computational modeling using Discovery Studio 2016.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"129-137"},"PeriodicalIF":0.3,"publicationDate":"2016-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329568","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-12-20DOI: 10.6564/JKMRS.2016.20.4.114
Keunhong Jeong
Nitrogen vacancy-centered diamond has recently emerged as a promising material for various applications due to its special optical and magnetic properties. In particular, its applications as a fluorescent biomarker with small toxicity, magnetic field and electric field sensors have been a topic of great interest. Recent review (R. Schirhagl et al 2014) introduced those applications using single NV-center in nanodiamond. In this minireview, I introduce the rapidly emerging DNP (Dynamic Nuclear Polarization) field using optically-pumped NV center in diamonds. Additionally, the possibility of exploiting the optically-pumped NV center for polarization transfer source, which will produce a profound impact on room temperature DNP, will be discussed.
氮空位中心金刚石由于其特殊的光学和磁性能，近年来成为一种具有广泛应用前景的材料。特别是其作为小毒性荧光生物标志物、磁场和电场传感器的应用一直是人们非常感兴趣的话题。最近的综述(R. Schirhagl et al 2014)介绍了在纳米金刚石中使用单个nv中心的应用。在这篇小型综述中，我介绍了在金刚石中利用光泵浦NV中心迅速出现的DNP(动态核极化)场。此外，还讨论了利用光抽运NV中心作为偏振转移源的可能性，这将对室温DNP产生深远的影响。
{"title":"Minireview on Nuclear Spin Polarization in Optically-Pumped Diamond Nitrogen Vacancy Centers","authors":"Keunhong Jeong","doi":"10.6564/JKMRS.2016.20.4.114","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.4.114","url":null,"abstract":"Nitrogen vacancy-centered diamond has recently emerged as a promising material for various applications due to its special optical and magnetic properties. In particular, its applications as a fluorescent biomarker with small toxicity, magnetic field and electric field sensors have been a topic of great interest. Recent review (R. Schirhagl et al 2014) introduced those applications using single NV-center in nanodiamond. In this minireview, I introduce the rapidly emerging DNP (Dynamic Nuclear Polarization) field using optically-pumped NV center in diamonds. Additionally, the possibility of exploiting the optically-pumped NV center for polarization transfer source, which will produce a profound impact on room temperature DNP, will be discussed.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"114-120"},"PeriodicalIF":0.3,"publicationDate":"2016-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329550","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-12-20DOI: 10.6564/JKMRS.2016.20.4.138
Sungjin Lee, Chin-Ju Park
Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.
{"title":"Backbone Assignment of the N-terminal Domain of Human Replication Protein A 70 kDa","authors":"Sungjin Lee, Chin-Ju Park","doi":"10.6564/JKMRS.2016.20.4.138","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.4.138","url":null,"abstract":"Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"138-142"},"PeriodicalIF":0.3,"publicationDate":"2016-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-09-20DOI: 10.6564/JKMRS.2016.20.3.076
Ja-shil Hyun, Sung Jean Park
{"title":"Dynamic Profile of the Copper Chaperone CopP from Helicobacter Pylori Depending on the Bound Metals","authors":"Ja-shil Hyun, Sung Jean Park","doi":"10.6564/JKMRS.2016.20.3.076","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.3.076","url":null,"abstract":"","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"76-81"},"PeriodicalIF":0.3,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329989","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-09-20DOI: 10.6564/JKMRS.2016.20.3.066
Min-Gyu Kim, Tae-Hoan Shin, Seo-Ree Choi, Jae-Gyu Choi, Joon-Hwa Lee
The replication protein A (RPA), is a heterotrimer with 70, 32 and 14 kDa subunits and plays a crucial role in DNA replication, recombination, and repair. The largest subunit, RPA70, binds to single-stranded DNA (ssDNA) and mediates interactions with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various temperatures, to understand the temperature dependency of ssDNA binding affinity of RPA70A. Essential residues for ssDNA binding were conserved while less essential parts were changed with the temperature. Our results provide valuable insights into the molecular mechanism of the ssDNA binding of human RPA.
{"title":"NMR Study of Temperature-Dependent Single-Stranded DNA Binding Affinity of Human Replication Protein A","authors":"Min-Gyu Kim, Tae-Hoan Shin, Seo-Ree Choi, Jae-Gyu Choi, Joon-Hwa Lee","doi":"10.6564/JKMRS.2016.20.3.066","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.3.066","url":null,"abstract":"The replication protein A (RPA), is a heterotrimer with 70, 32 and 14 kDa subunits and plays a crucial role in DNA replication, recombination, and repair. The largest subunit, RPA70, binds to single-stranded DNA (ssDNA) and mediates interactions with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various temperatures, to understand the temperature dependency of ssDNA binding affinity of RPA70A. Essential residues for ssDNA binding were conserved while less essential parts were changed with the temperature. Our results provide valuable insights into the molecular mechanism of the ssDNA binding of human RPA.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"66-70"},"PeriodicalIF":0.3,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329821","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-09-20DOI: 10.6564/JKMRS.2016.20.3.082
Dahye Yoon, Ick-Hyun Jo, Suhkmann Kim
Abstract Ginseng is used as a medicinal ingredient. The quality control of species, age, origin and manufacturing process is important. The metabolome of ginseng about quality was studied in many reports. Almost studies carried out the extract of ginseng, however, the reproducibility cannot be obtained using extracted sample. In this study, powdery ginseng samples were analyzed using high resolution-magic angle spinning nuclear magnetic resonance (HR-MAS NMR)-based metabolomics except extraction step. Sample was measured three times using 600 MHz NMR spectrometer equipped with nano probe. Reproducibility can be enhanced using this method and the metabolic profiles of ginseng were identified and quantified.
{"title":"HR-MAS NMR Technique for Metabolic Profiling of Powdery Ginseng","authors":"Dahye Yoon, Ick-Hyun Jo, Suhkmann Kim","doi":"10.6564/JKMRS.2016.20.3.082","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.3.082","url":null,"abstract":"Abstract Ginseng is used as a medicinal ingredient. The quality control of species, age, origin and manufacturing process is important. The metabolome of ginseng about quality was studied in many reports. Almost studies carried out the extract of ginseng, however, the reproducibility cannot be obtained using extracted sample. In this study, powdery ginseng samples were analyzed using high resolution-magic angle spinning nuclear magnetic resonance (HR-MAS NMR)-based metabolomics except extraction step. Sample was measured three times using 600 MHz NMR spectrometer equipped with nano probe. Reproducibility can be enhanced using this method and the metabolic profiles of ginseng were identified and quantified.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"82-86"},"PeriodicalIF":0.3,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71330005","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-09-20DOI: 10.6564/JKMRS.2016.20.3.087
S. Lee
Although NMR technique has been using in many areas of chemistry, its merit on quantitative analysis seems not to acknowledge greatly because of the many inferior intrinsic aspects, particularly its sensitivity. Recently, new NMR techniques, high-field NMR, and demands for cutting edge techniques of analysis, however, seem to change the role of NMR spectroscopy in this field. This review shows the application of NMR development in quantitative analysis and will discuss the basic idea, limitations, and pitfalls. Then it will show you several successful applications applied in quantitative analysis and you will see how useful and accurate method it is.
{"title":"The Role of NMR in the Field of Quantitative Analysis","authors":"S. Lee","doi":"10.6564/JKMRS.2016.20.3.087","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.3.087","url":null,"abstract":"Although NMR technique has been using in many areas of chemistry, its merit on quantitative analysis seems not to acknowledge greatly because of the many inferior intrinsic aspects, particularly its sensitivity. Recently, new NMR techniques, high-field NMR, and demands for cutting edge techniques of analysis, however, seem to change the role of NMR spectroscopy in this field. This review shows the application of NMR development in quantitative analysis and will discuss the basic idea, limitations, and pitfalls. Then it will show you several successful applications applied in quantitative analysis and you will see how useful and accurate method it is.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"87-94"},"PeriodicalIF":0.3,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2016-09-20DOI: 10.6564/JKMRS.2016.20.3.071
Min-Woo Lee, Jungyuen Choi, Jae-Gyu Choi, Ae-Ree Lee, Joon-Hwa Lee
The replication protein A (RPA) plays a crucial role in DNA replication, recombination, and repair. RPA consists of 70, 32 and 14 kDa subunits and has high single-stranded DNA (ssDNA) binding affinity. The largest subunit, RPA70, mainly contributes to bind to ssDNA as well as interact with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various pH, to understand the effect of pH on the ssDNA binding of RPA70A. The chemical shift perturbations of binding residues were most significant at pH 6.5 and they reduced with pH increment. This study provides valuable insights into the molecular mechanism of the ssDNA binding of human RPA.
{"title":"NMR Study of the pH Effect on the DNA Binding Affinity of Human RPA","authors":"Min-Woo Lee, Jungyuen Choi, Jae-Gyu Choi, Ae-Ree Lee, Joon-Hwa Lee","doi":"10.6564/JKMRS.2016.20.3.071","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.3.071","url":null,"abstract":"The replication protein A (RPA) plays a crucial role in DNA replication, recombination, and repair. RPA consists of 70, 32 and 14 kDa subunits and has high single-stranded DNA (ssDNA) binding affinity. The largest subunit, RPA70, mainly contributes to bind to ssDNA as well as interact with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various pH, to understand the effect of pH on the ssDNA binding of RPA70A. The chemical shift perturbations of binding residues were most significant at pH 6.5 and they reduced with pH increment. This study provides valuable insights into the molecular mechanism of the ssDNA binding of human RPA.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"71-75"},"PeriodicalIF":0.3,"publicationDate":"2016-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329830","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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