{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T11:10:46Z","timestamp":1790334646126,"version":"4.1.0"},"reference-count":80,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:00:00Z","timestamp":1790294400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:00:00Z","timestamp":1790294400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100000035","name":"Institute of Nutrition, Metabolism and Diabetes","doi-asserted-by":"publisher","award":["PJT\u2010178246"],"award-info":[{"award-number":["PJT\u2010178246"]}],"id":[{"id":"10.13039\/501100000035","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Letters"],"abstract":"<jats:p>Nanobodies, the single\u2010domain antigen\u2010binding fragments derived from camelid heavy chain antibodies, have emerged as powerful tools in structural biology. Their small size, high stability, and ability to bind with exceptional specificity make them ideal for applications in nuclear magnetic resonance (NMR) spectroscopy. In protein NMR, nanobodies can serve as chaperones to stabilize flexible regions, reduce conformational heterogeneity, and enhance spectral quality. They facilitate the study of challenging targets such as membrane proteins, large complexes, and intrinsically disordered proteins by improving solubility and enabling selective labeling strategies. Furthermore, nanobody\u2010assisted NMR spectroscopy provides unique opportunities for probing dynamic interactions and conformational states under near\u2010physiological conditions. This review summarizes recent advances in nanobody engineering for NMR studies, including the synthetic nanobodies, highlights the nanobodies'\u00a0role in overcoming size and stability limitations, and discusses future directions for integrating nanobodies into emerging NMR methodologies, with an emphasis on protein dynamics and protein\u2013protein interactions in the context of drug discovery.<\/jats:p>","DOI":"10.1002\/1873-3468.70473","type":"journal-article","created":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T10:48:59Z","timestamp":1790333339000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Smaller is better: nanobodies meet\n                    <scp>NMR<\/scp>"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1307-5063","authenticated-orcid":false,"given":"Oleg Y.","family":"Dmitriev","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Microbiology and Immunology University of Saskatchewan  Saskatoon Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,25]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001120","article-title":"A case of convergence: why did a simple alternative to canonical antibodies arise in sharks and camels?","volume":"9","author":"Flajnik MF","year":"2011","journal-title":"PLoS Biol"},{"key":"e_1_2_7_3_1","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/374168a0","article-title":"A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks","volume":"374","author":"Greenberg AS","year":"1995","journal-title":"Nature"},{"key":"e_1_2_7_4_1","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1038\/363446a0","article-title":"Naturally occurring antibodies devoid of light chains","volume":"363","author":"Hamers\u2010Casterman 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