Pub Date : 2017-06-20DOI: 10.6564/JKMRS.2017.21.2.072
Jeongmin Oh, Soo-Ho Choi, J. Yun, Yoon-Joo Ko, Kang-Yell Choi, Weontae Lee
{"title":"Cloning, Purification and NMR Studies on β-catenin C-terminal Domain","authors":"Jeongmin Oh, Soo-Ho Choi, J. Yun, Yoon-Joo Ko, Kang-Yell Choi, Weontae Lee","doi":"10.6564/JKMRS.2017.21.2.072","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.2.072","url":null,"abstract":"","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"72-77"},"PeriodicalIF":0.3,"publicationDate":"2017-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41944512","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 : 2017-06-20DOI: 10.6564/JKMRS.2017.21.2.063
A. Lim
{"title":"Paraelectric-Ferroelectric Phase Transition of (NH4)2SO4 Single Crystals by 14N NMR","authors":"A. Lim","doi":"10.6564/JKMRS.2017.21.2.063","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.2.063","url":null,"abstract":"","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"63-66"},"PeriodicalIF":0.3,"publicationDate":"2017-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43367739","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 : 2017-06-20DOI: 10.6564/JKMRS.2017.21.2.067
S. Park, A. Lim
{"title":"Role of NH4 and H2O in Tutton Salt (NH4)2M(SO4)2·6H2O (M=Fe and Zn) Single Crystals Studied by 1H and 14N NMR at High Temperatures","authors":"S. Park, A. Lim","doi":"10.6564/JKMRS.2017.21.2.067","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.2.067","url":null,"abstract":"","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"67-71"},"PeriodicalIF":0.3,"publicationDate":"2017-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48361858","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 : 2017-03-20DOI: 10.6564/JKMRS.2017.21.1.026
Jong-Jae Yi, Won-Je Kim, J. Rhee, Jongsoo Lim, Bong‐Jin Lee, W. Son
Dynamic properties of proteins can present key information on protein-ligand and protein-protein interaction. Despite their usefulness, the properties of protein dynamics have not been obtained easily due to protein stability and short-term measurement. Here, it is shown that combined method for analysis of dynamical properties. It utilizes predicted order parameter and NMR relaxation data such as T 1 , T 2 , and heteronuclear NOE. The suggested method could be used to know the flexibility of protein roughly without precise dynamical parameters such as order parameters through model-free analysis.
{"title":"Elucidating the Dynamic Properties of Globular Protein using Predicted Order Parameters and 15N NMR Relaxation","authors":"Jong-Jae Yi, Won-Je Kim, J. Rhee, Jongsoo Lim, Bong‐Jin Lee, W. Son","doi":"10.6564/JKMRS.2017.21.1.026","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.1.026","url":null,"abstract":"Dynamic properties of proteins can present key information on protein-ligand and protein-protein interaction. Despite their usefulness, the properties of protein dynamics have not been obtained easily due to protein stability and short-term measurement. Here, it is shown that combined method for analysis of dynamical properties. It utilizes predicted order parameter and NMR relaxation data such as T 1 , T 2 , and heteronuclear NOE. The suggested method could be used to know the flexibility of protein roughly without precise dynamical parameters such as order parameters through model-free analysis.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"26-30"},"PeriodicalIF":0.3,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46776099","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 : 2017-03-20DOI: 10.6564/JKMRS.2017.21.1.013
H. Won
Human sterol Δ8-Δ7 isomerase, commonly known as emopamil binding protein (EBP), is an essential protein in the cholesterol-synthetic pathway, and mutations of this protein are critically associated with human diseases such as Conradi-Hunermann–Happle or male EBP disorder with neurological defects syndrome. Due to such a clinical importance, EBP has been intensively investigated and some important features have been reported. EBP is a tetra-spanning membrane protein, of which 2 nd , 3 rd , and 4 th membrane-spanning α helices play an important role in its enzymatic function. However, detailed structural feature at atomic resolution has not yet been elucidated, due to characteristic difficulties in dealing with membrane protein. Here, we over-expressed EBP using Escherichia coli and performed detergent screening to find suitable membrane mimetics for structural studies of the protein by NMR. As results, DPC and LMPG could be evaluated as the most favorable detergents to acquire promising NMR spectra for structural study of EBP. receptor σ-ligand SR31747A, trifuoperazine,
{"title":"Detergent Screening for NMR-Based Structural Study of the Integral Membrane Protein, Emopamil Binding Protein (Human Sterol Δ8-Δ7 Isomerase)","authors":"H. Won","doi":"10.6564/JKMRS.2017.21.1.013","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.1.013","url":null,"abstract":"Human sterol Δ8-Δ7 isomerase, commonly known as emopamil binding protein (EBP), is an essential protein in the cholesterol-synthetic pathway, and mutations of this protein are critically associated with human diseases such as Conradi-Hunermann–Happle or male EBP disorder with neurological defects syndrome. Due to such a clinical importance, EBP has been intensively investigated and some important features have been reported. EBP is a tetra-spanning membrane protein, of which 2 nd , 3 rd , and 4 th membrane-spanning α helices play an important role in its enzymatic function. However, detailed structural feature at atomic resolution has not yet been elucidated, due to characteristic difficulties in dealing with membrane protein. Here, we over-expressed EBP using Escherichia coli and performed detergent screening to find suitable membrane mimetics for structural studies of the protein by NMR. As results, DPC and LMPG could be evaluated as the most favorable detergents to acquire promising NMR spectra for structural study of EBP. receptor σ-ligand SR31747A, trifuoperazine,","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"13-19"},"PeriodicalIF":0.3,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44596389","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 : 2017-03-20DOI: 10.6564/JKMRS.2017.21.1.031
Sujin Lee, Sunmi Kang, Sunghyouk Park
Together with radiotherapy, chemotherapy using cytotoxic agents is one of the most common therapies in cancer. Metabolic changes in cancer cells are drawing much attention recently, but the metabolic alterations by anticancer agents have not been much studied. Here, we investigated the effects of commonly used cytotoxic agents on lung normal cell MRC5 and lung cancer cell A549. We employed cis-plastin, doxorubicin, and 5-Fluorouracil and compared their effects on the viability and metabolism of the normal and cancer cell lines. We first established the concentration of the cytotoxic reagents that give differences in the viabilities of normal and cancer cell lines. In those conditions, the viability of A549 decreased significantly, whereas that of MRC5 remained unchanged. To study the metabolic alterations implicated in the viability differences, we obtained the metabolic profiles using 1 H-NMR spectrometry. The 1 H-NMR data showed that the metabolic changes of A549 cells are more remarkable than that of MRC5 cells and the effect of 5-FU on the A549 cells is the most distinct compared to other treatments. Heat map analysis showed that metabolic alterations under treatment of cytotoxic agents are totally different between normal and cancer cells. Multivariate analysis and weighted correlation network analysis (WGCNA) revealed a distinctive metabolite signature and hub metabolites. Two different analysis tools revealed that the changes of cell metabolism in response to cytotoxic agents were highly correlated with the Warburg effect and Reductive lipogenesis, two pathways having important effects on the cell survival. Taken together, our study addressed the correlation between the viability and metabolic profiles of MRC5 and A549 cells upon the treatment of cytotoxic anticancer agents.
{"title":"Comparison of Metabolic Profiles of Normal and Cancer Cells in Response to Cytotoxic Agents","authors":"Sujin Lee, Sunmi Kang, Sunghyouk Park","doi":"10.6564/JKMRS.2017.21.1.031","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.1.031","url":null,"abstract":"Together with radiotherapy, chemotherapy using cytotoxic agents is one of the most common therapies in cancer. Metabolic changes in cancer cells are drawing much attention recently, but the metabolic alterations by anticancer agents have not been much studied. Here, we investigated the effects of commonly used cytotoxic agents on lung normal cell MRC5 and lung cancer cell A549. We employed cis-plastin, doxorubicin, and 5-Fluorouracil and compared their effects on the viability and metabolism of the normal and cancer cell lines. We first established the concentration of the cytotoxic reagents that give differences in the viabilities of normal and cancer cell lines. In those conditions, the viability of A549 decreased significantly, whereas that of MRC5 remained unchanged. To study the metabolic alterations implicated in the viability differences, we obtained the metabolic profiles using 1 H-NMR spectrometry. The 1 H-NMR data showed that the metabolic changes of A549 cells are more remarkable than that of MRC5 cells and the effect of 5-FU on the A549 cells is the most distinct compared to other treatments. Heat map analysis showed that metabolic alterations under treatment of cytotoxic agents are totally different between normal and cancer cells. Multivariate analysis and weighted correlation network analysis (WGCNA) revealed a distinctive metabolite signature and hub metabolites. Two different analysis tools revealed that the changes of cell metabolism in response to cytotoxic agents were highly correlated with the Warburg effect and Reductive lipogenesis, two pathways having important effects on the cell survival. Taken together, our study addressed the correlation between the viability and metabolic profiles of MRC5 and A549 cells upon the treatment of cytotoxic anticancer agents.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"31-43"},"PeriodicalIF":0.3,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46913658","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 : 2017-03-20DOI: 10.6564/JKMRS.2017.21.1.020
Ko On Lee, J. Suh
The cytoplasmic domains A and B of the mannitol transporter enzyme II Mtl are covalently linked in Escherichia coli , but separately expressed in Thermoanaerobacter Tengcongensis . The phosphorylation of domain B ( Tt IIB Mtl ) substantially increases the binding affinity to the domain A ( Tt IIA Mtl ) in T. Tengcongensis . To understand the structural basis of the enhanced domain - domain interaction by protein phosphorylation, we obtained NMR backbone assignments of the phospho- Tt IIB Mtl using a standard suite of triple resonance experiments. Our results will be useful to monitor chemical shift changes at the active site of phosphorylation and the binding interfaces.
{"title":"Backbone Assignment of Phosphorylated Cytoplasmic Domain B of Mannitol Transporter IIMtl in Thermoanaerobacter Tengcongensis","authors":"Ko On Lee, J. Suh","doi":"10.6564/JKMRS.2017.21.1.020","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.1.020","url":null,"abstract":"The cytoplasmic domains A and B of the mannitol transporter enzyme II Mtl are covalently linked in Escherichia coli , but separately expressed in Thermoanaerobacter Tengcongensis . The phosphorylation of domain B ( Tt IIB Mtl ) substantially increases the binding affinity to the domain A ( Tt IIA Mtl ) in T. Tengcongensis . To understand the structural basis of the enhanced domain - domain interaction by protein phosphorylation, we obtained NMR backbone assignments of the phospho- Tt IIB Mtl using a standard suite of triple resonance experiments. Our results will be useful to monitor chemical shift changes at the active site of phosphorylation and the binding interfaces.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"20-25"},"PeriodicalIF":0.3,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49321487","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 : 2017-03-20DOI: 10.6564/JKMRS.2017.21.1.07
P. Park, Wan-Seop Kim, S. Joo, Hyung-Kew Lee
The nuclear magnetic resonance (NMR) and atomic magnetic resonance (AMR) plays a fundamental role in achieving a high accuracy of magnetic field measurements. Magnetic field unit (T) was realized based on the shielded proton gyromagnetic ratio ( γ ' P ), helium-4 gyromagnetic ratio ( γ 4He ) and related techniques. The magnetic field standard system has been disseminated by the NMR magnetometer and electromagnet, a Helmholtz coil system, and AMR magnetometer in the nonmagnetic laboratory. A magnetic field standard below 1 mT has been developed by using Cs and Cs- 4 He AMR with automatic compensation of an external magnetic field noise. The standards serve for the calibration of magnetometers and support the test of sensors and materials in the range from 5 μT to 2.0 T with (1 to 50) μT/T uncertainty ( k =2).
核磁共振（NMR）和原子磁共振（AMR）在实现高精度磁场测量方面发挥着重要作用。磁场单元（T）是基于屏蔽质子旋磁比（γ′P）、氦-4旋磁比和相关技术实现的。在非磁性实验室中，核磁共振磁强计和电磁铁、亥姆霍兹线圈系统和AMR磁强计已经传播了磁场标准系统。通过使用Cs和Cs-4 He AMR并自动补偿外部磁场噪声，开发了低于1mT的磁场标准。该标准用于磁强计的校准，并支持在5μT至2.0 T范围内对传感器和材料进行测试，不确定度为（1至50）μT/T（k=2）。
{"title":"Magnetic Field Standards Using Magnetic Resonance","authors":"P. Park, Wan-Seop Kim, S. Joo, Hyung-Kew Lee","doi":"10.6564/JKMRS.2017.21.1.07","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.1.07","url":null,"abstract":"The nuclear magnetic resonance (NMR) and atomic magnetic resonance (AMR) plays a fundamental role in achieving a high accuracy of magnetic field measurements. Magnetic field unit (T) was realized based on the shielded proton gyromagnetic ratio ( γ ' P ), helium-4 gyromagnetic ratio ( γ 4He ) and related techniques. The magnetic field standard system has been disseminated by the NMR magnetometer and electromagnet, a Helmholtz coil system, and AMR magnetometer in the nonmagnetic laboratory. A magnetic field standard below 1 mT has been developed by using Cs and Cs- 4 He AMR with automatic compensation of an external magnetic field noise. The standards serve for the calibration of magnetometers and support the test of sensors and materials in the range from 5 μT to 2.0 T with (1 to 50) μT/T uncertainty ( k =2).","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"7-12"},"PeriodicalIF":0.3,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43689624","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 : 2017-03-20DOI: 10.6564/JKMRS.2017.21.1.01
Im Jonghyuk, J. H. Lee
Enhancements in NMR sensitivity have been the main driving force to extend the boundaries of NMR applications. Recently, techniques to shift the thermally populated nuclear spin states are employed to gain high NMR signals. Here, we introduce a technique called photochemically induced dynamic nuclear polarization (photo-CIDNP) and discuss its progresses in enhancing the solution-state NMR sensitivity.
{"title":"Sensitivity Enhancement in Solution NMR via Photochemically Induced Dynamic Nuclear Polarization","authors":"Im Jonghyuk, J. H. Lee","doi":"10.6564/JKMRS.2017.21.1.01","DOIUrl":"https://doi.org/10.6564/JKMRS.2017.21.1.01","url":null,"abstract":"Enhancements in NMR sensitivity have been the main driving force to extend the boundaries of NMR applications. Recently, techniques to shift the thermally populated nuclear spin states are employed to gain high NMR signals. Here, we introduce a technique called photochemically induced dynamic nuclear polarization (photo-CIDNP) and discuss its progresses in enhancing the solution-state NMR sensitivity.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"1-6"},"PeriodicalIF":0.3,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41646629","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.2016.20.4.102
J. Jee
With the rapid increase of data on protein-protein interactions, the need for delineating the 3D structures of huge protein complexes has increased. The protocols for determining nuclear magnetic resonance (NMR) structure can be applied to modeling complex structures coupled with sparse experimental restraints. In this report, I suggest the use of multiple rigid bodies for improving the efficiency of NMR-assisted structure modeling of huge complexes using CYANA. By preparing a region of known structure as a new type of residue that has no torsion angle, one can facilitate the search of the conformational spaces. This method has a distinct advantage over the rigidification of a region with synthetic distance restraints, particularly for the calculation of huge molecules. I have demonstrated the idea with calculations of decaubiquitins that are linked via Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, or Lys63, or head to tail. Here, the ubiquitin region consisting of residues 1‒70 was treated as a rigid body with a new residue. The efficiency of the calculation was further demonstrated in Lys48-linked decaubiquitin with ambiguous distance restraints. The approach can be readily extended to either protein-protein complexes or large proteins consisting of several domains.
{"title":"Strategy for Determining the Structures of Large Biomolecules using the Torsion Angle Dynamics of CYANA","authors":"J. Jee","doi":"10.6564/JKMRS.2016.20.4.102","DOIUrl":"https://doi.org/10.6564/JKMRS.2016.20.4.102","url":null,"abstract":"With the rapid increase of data on protein-protein interactions, the need for delineating the 3D structures of huge protein complexes has increased. The protocols for determining nuclear magnetic resonance (NMR) structure can be applied to modeling complex structures coupled with sparse experimental restraints. In this report, I suggest the use of multiple rigid bodies for improving the efficiency of NMR-assisted structure modeling of huge complexes using CYANA. By preparing a region of known structure as a new type of residue that has no torsion angle, one can facilitate the search of the conformational spaces. This method has a distinct advantage over the rigidification of a region with synthetic distance restraints, particularly for the calculation of huge molecules. I have demonstrated the idea with calculations of decaubiquitins that are linked via Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, or Lys63, or head to tail. Here, the ubiquitin region consisting of residues 1‒70 was treated as a rigid body with a new residue. The efficiency of the calculation was further demonstrated in Lys48-linked decaubiquitin with ambiguous distance restraints. The approach can be readily extended to either protein-protein complexes or large proteins consisting of several domains.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"20 1","pages":"102-108"},"PeriodicalIF":0.3,"publicationDate":"2016-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71329932","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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