{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T14:19:48Z","timestamp":1787581188515,"version":"build-2736575974"},"reference-count":61,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T00:00:00Z","timestamp":1787529600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int. J. Mol. Sci.","IJMS"],"abstract":"<jats:p>Protein\u2013ligand interactions are fundamental to physiological processes and drug discovery. Based on the types of information on protein\u2013ligand interactions provided by nuclear magnetic resonance (NMR) experiments, these NMR experiments can be categorized into three distinct classes: (i) molecular-level qualitative binding detection, (ii) residue-level mapping of binding interfaces, and (iii) atomic-level structure determination and conformational dynamics of protein\u2013ligand complexes. This hierarchy enables a workflow that accelerates the progression from initial binding identification to structural and dynamic characterization. In this review, we discuss how these experiments characterize molecular recognition. Notably, the term \u201cligand\u201d in this article refers exclusively to small molecules.<\/jats:p>","DOI":"10.3390\/ijms27177561","type":"journal-article","created":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T13:20:43Z","timestamp":1787577643000},"page":"7561","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["NMR Studies on Protein\u2013Ligand Interactions"],"prefix":"10.3390","volume":"27","author":[{"given":"Haiqin","family":"Yao","sequence":"first","affiliation":[{"name":"School of Life Sciences, Tsinghua University, Beijing 100084, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ning","family":"Xu","sequence":"additional","affiliation":[{"name":"Technology Center for Protein Sciences, Tsinghua University, Beijing 100084, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/bs.mie.2018.09.003","article-title":"Identification of Unknown Metabolomics Mixture Compounds by Combining NMR, MS, and Cheminformatics","volume":"615","author":"Leggett","year":"2019","journal-title":"Methods Enzymol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"eads9530","DOI":"10.1126\/science.ads9530","article-title":"Deep contrastive learning enables genome-wide virtual screening","volume":"391","author":"Jia","year":"2026","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/s43586-023-00199-x","article-title":"Isothermal titration calorimetry","volume":"3","author":"Bastos","year":"2023","journal-title":"Nat. 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