Protein-ligand interactions studied by NMR

Hidekazu Hiroaki, Daisuke Kohda

    Research output: Chapter in Book/Report/Conference proceedingChapter

    1 Citation (Scopus)


    Various solution NMR experiments for studying protein-ligand interactions have become indispensable techniques in both academia and industry. In general, solution NMR is superior to other physico-chemical methods, in terms of its spatial resolution and the fact that protein modifications are not required. The applications are loosely classified into two categories, "ligand-based approach" and "protein-based approach." Many unique experiments have been developed for the ligand-based approach, including STD, WaterLOGSY, DIRECTION, INPHARMA, ILOE, and trNOE. These experiments frequently comprise the important steps of a drug-discovery process, including ligand screening, pharmacophore mapping, and molecular design. This review provides a practicable classification of these experiments, to promote the selection of a suitable experiment depending on the purpose. In contrast, the variation of experiments in the protein-based approach is rather limited. The 1H-15N-HSQC-based NMR titration experiment and its variants are preferentially used for analyses of protein-ligand interactions. This review also discusses several practical aspects of the NMR titration experiment, including sample handling and data acquisition and analysis.

    Original languageEnglish
    Title of host publicationExperimental Approaches of NMR Spectroscopy
    Subtitle of host publicationMethodology and Application to Life Science and Materials Science
    PublisherSpringer Singapore
    Number of pages22
    ISBN (Electronic)9789811059667
    ISBN (Print)9789811059650
    Publication statusPublished - Nov 23 2017

    All Science Journal Classification (ASJC) codes

    • General Chemistry
    • General Biochemistry,Genetics and Molecular Biology
    • General Engineering
    • General Materials Science


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