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High-Field Nuclear Magnetic Resonance

High-Field Nuclear Magnetic Resonance Leading-edge Equipment Home

Equipment Introduction

900 MHz Nuclear Magnetic Resonance Spectrometer is a core equipment for the study of biomolecular structure and development of new drugs which is installed in Ochang Center. It is utilized as a national collaborative research equipment.

Characteristics of the Equipment

  • The sensitivity of the cryogenic probe to 1H is more than 4 times (8,000) that of conventional room temperature probe, so the experiment time can be shortened to 1/16
  • Protein structural studies can be performed with 100 μM or lower concentration samples
  • Minimum mass for 13C experiment of natural products is about 100 μg

Representative Research Case

Target Search Pathways Visualized by Paramagnetic NMR Spectroscopy

NMR paramagnetic relaxation enhancement have been employed to visualize the encounter complexes between histidine-containing phosphocarrier protein and the N-terminal domain of enzyme I and demonstrate that protein association can be significantly enhanced by engineering on-pathways.

Paramagnetic NMR spectroscopy visualizes the protein target search process

Application

  • J-based configuration analysis of natural compound
  • Self assembly and DOSY NMR of the molecular knot and macrocycle

Representative Research Papers

  • The First Quantitative Synthesis of a Closed Three-Link Chain (613) Using Coordination and Noncovalent Interactions-Driven Self-Assembly
    Jatinder Singh, Dong Hwan Kim, Eun-Hee Kim, Hyunuk Kim, Rizky Hadiputra, Jaehoon Jung, and Ki-Whan Chi
    Journal of the American Chemical Society 2020 142 (20), 9327-9336 doi: 10.1021/jacs.0c01406
  • Single-Molecule-Based Detection of Conserved Influenza A Virus RNA Promoter Using a Protein Nanopore
    Sohee Oh, Mi-Kyung Lee, and Seung-Wook Chi
    ACS Sensors 2019 4 (11), 2849-2853 DOI: 10.1021/acssensors.9b01558
  • Tyrosine 51 Residue of the syndecan-2 Extracellular Domain Is Involved in the Interaction With and Activation of Pro-Matrix metalloproteinase-7
    Bohee Jang, Ji-Hye Yun, Sojoong Choi, Jimin Park, Dong Hae Shin, Seung-Taek Lee, Weontae Lee, Eok-Soo Oh,
    Sci Rep. 2019 Jul 23;9(1):10625. doi: 10.1038/s41598-019-47140-5
  • Investigation of the core binding regions of human Werner syndrome and Fanconi anemia group J helicases on replication protein A
    Yeom, G., Kim, J. & Park, C.,
    Sci Rep 9, 14016 (2019). https://doi.org/10.1038/s41598-019-50502-8
  • Facilitated Protein Association via Engineered Target Search Pathways Visualized by Paramagnetic NMR Spectroscopy
    An S.Y., Kim E.-H., Suh J.-Y.,
    Structure, 2018, 26 (6), pp 887-89300, doi:10.1016/j.str.2018.04.009
  • Diverse Metabolite Variations in Tea (Camellia sinensis L.) Leaves Grown under Various Shade Conditions Revisited: A Metabolomics Study
    Ji H.-G., Lee Y.-R., Lee M.-S., Hwang K.H., Park C.Y., Kim E.-H., Park J.S., Hong Y.-S.,
    Journal of Agricultural and Food Chemistry, 2018, 66 (8), pp 1889-1897, doi:10.1021/acs.jafc.7b04768
  • Coordination-Driven Self-Assembly of Heterotrimetallic Barrel and Bimetallic Cages Using a Cobalt Sandwich-Based Tetratopic Donor
    Singh N., Singh J., Kim D., Kim D.H., Kim E.-H., Lah M.S., Chi K.-W.,
    Inorganic Chemistry, 2018, 57 (7), pp 3521-3528, doi:10.1021/acs.inorgchem.7b02653
  • Determination of the Absolute Configuration of Polyhydroxy Compound Ostreol B Isolated from the Dinoflagellate Ostreopsis cf. ovata
    Hwang B.S., Yoon E.Y., Jeong E.J., Park J., Kim E.-H., Rho J.-R.,
    Journal of Organic Chemistry, 2018, 83 (1), pp 194-202, doi:10.1021/acs.joc.7b02569
  • Evidence of link between quorum sensing and sugar metabolism in Escherichia coli revealed via cocrystal structures of LsrK and HPr
    Ha J.-H., Hauk P., Cho K., Eo Y., Ma X., Stephens K., Cha S., Jeong M., Suh J.-Y., Sintim H.O., Bentley W.E., Ryu K.-S.,
    Science Advances, 2018, 4 (6), eaar7063, doi:10.1126/sciadv.aar7063
  • Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone
    Kim J., Choi D., Cha S.-Y., Oh Y.-M., Hwang E., Park C., Ryu K.-S.,
    Journal of Molecular Biology, 2018, 430 (12), pp 1760-1772, doi:10.1016/j.jmb.2018.04.029