{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T09:21:16Z","timestamp":1789118476746,"version":"build-2803163510"},"reference-count":210,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T00:00:00Z","timestamp":1789084800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Biosci."],"abstract":"<jats:p>Structural biology is moving beyond the determination of static molecular structures toward quantitative descriptions of biomolecular mechanisms. Modern questions increasingly focus on conformational heterogeneity, exchange kinetics, weak and transient interactions, allostery, disorder, assembly, and phase behavior. These properties are often difficult to infer from crystallography, cryo-electron microscopy, scattering, imaging, mass spectrometry, molecular simulations, or structural prediction alone. Solution NMR spectroscopy occupies a distinctive position in this integrated landscape because it provides residue- and atom-specific observables that report on structure, dynamics, populations, kinetics, and interactions directly in solution. Here, we review the role of solution NMR in integrated structural biology from a question-centered perspective. Rather than organizing the discussion around individual NMR experiments, we ask how NMR can be used with complementary approaches to address recurring mechanistic problems: What is the structure of a biomolecule in solution? What conformational states are populated, and how rapidly do they interconvert? How do ligands, nucleic acids, membranes, surfaces, or partner proteins bind? How are allosteric signals transmitted? How do disorder, large assemblies, and biomolecular condensates regulate function? How can NMR observables be integrated with simulations and other structural restraints to build testable models? The future of solution NMR lies not primarily in isolated structure determination, but in its ability to transform structural models into dynamic, quantitative, and experimentally constrained descriptions of biomolecular mechanism.<\/jats:p>","DOI":"10.3389\/fmolb.2026.1941622","type":"journal-article","created":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T08:55:19Z","timestamp":1789116919000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Beyond structures: solution NMR as the quantitative engine of integrated structural biology"],"prefix":"10.3389","volume":"13","author":[{"given":"Jeffrey A.","family":"Purslow","sequence":"first","affiliation":[{"name":"Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University","place":["Ames, IA, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincenzo","family":"Venditti","sequence":"additional","affiliation":[{"name":"Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University","place":["Ames, IA, United States"]},{"name":"Department of Chemistry, Iowa State University","place":["Ames, IA, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,9,11]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"12836","DOI":"10.1073\/pnas.2004317117","article-title":"A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle","volume":"117","author":"Abramov","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B2","doi-asserted-by":"publisher","first-page":"17817","DOI":"10.1021\/jacs.9b09002","article-title":"A unified description of intrinsically disordered protein dynamics under physiological conditions using NMR spectroscopy","volume":"141","author":"Adamski","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"B3","doi-asserted-by":"publisher","first-page":"107667","DOI":"10.1016\/j.jmr.2024.107667","article-title":"A delayed decoupling methyl-TROSY pulse sequence for atomic resolution studies of folded proteins and RNAs in condensates","volume":"362","author":"Ahmed","year":"2024","journal-title":"J. Magn. Reson"},{"key":"B4","doi-asserted-by":"publisher","first-page":"3583","DOI":"10.1038\/sj.emboj.7600366","article-title":"Cryo-electron microscopy of vitreous sections","volume":"23","author":"Al-Amoudi","year":"2004","journal-title":"EMBO J."},{"key":"B5","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","article-title":"Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"key":"B6","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/bs.mie.2020.06.009","article-title":"Methods for characterizing the material properties of biomolecular condensates","volume":"646","author":"Alshareedah","year":"2021","journal-title":"Methods Enzymol."},{"key":"B7","doi-asserted-by":"publisher","first-page":"2583","DOI":"10.1039\/d2na00099g","article-title":"Solution NMR methods for structural and thermodynamic investigation of nanoparticle adsorption equilibria","volume":"4","author":"An","year":"2022","journal-title":"Nanoscale Adv."},{"key":"B8","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1002\/0471140864.ps1716s72","article-title":"Neutron scattering techniques and applications in structural biology","volume":"17","author":"Ankner","year":"2013","journal-title":"Curr. Protoc. Protein Sci."},{"key":"B9","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1017\/S0033583514000122","article-title":"Visualizing transient dark states by NMR spectroscopy","volume":"48","author":"Anthis","year":"2015","journal-title":"Q. Rev. Biophys."},{"key":"B10","doi-asserted-by":"publisher","first-page":"5158","DOI":"10.1021\/acs.jmedchem.5b01447","article-title":"Protein-observed fluorine NMR: a bioorthogonal approach for small molecule discovery","volume":"59","author":"Arntson","year":"2016","journal-title":"J. Med. Chem."},{"key":"B11","doi-asserted-by":"publisher","first-page":"102768","DOI":"10.1016\/j.sbi.2023.102768","article-title":"Protein dynamics underlying allosteric regulation","volume":"84","author":"Astore","year":"2024","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B12","doi-asserted-by":"publisher","first-page":"1430","DOI":"10.1073\/pnas.0407146102","article-title":"Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein","volume":"102","author":"Bertoncini","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B13","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/j.tibs.2014.10.005","article-title":"How cryo-EM is revolutionizing structural biology","volume":"40","author":"Bai","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"B14","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B15","doi-asserted-by":"publisher","first-page":"e4578","DOI":"10.1002\/jms.4578","article-title":"Native mass spectrometry-A valuable tool in structural biology","volume":"55","author":"Barth","year":"2020","journal-title":"J. Mass Spectrom."},{"key":"B16","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1038\/s41596-024-01079-8","article-title":"Biolayer interferometry for measuring the kinetics of protein-protein interactions and nanobody binding","volume":"20","author":"Bates","year":"2025","journal-title":"Nat. Protoc."},{"key":"B17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1110\/ps.0233303","article-title":"Weak alignment offers new NMR opportunities to study protein structure and dynamics","volume":"12","author":"Bax","year":"2003","journal-title":"Protein Sci."},{"key":"B18","doi-asserted-by":"publisher","first-page":"5656","DOI":"10.1021\/ja069124n","article-title":"Structural characterization of flexible proteins using small-angle X-ray scattering","volume":"129","author":"Bernado","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"B19","doi-asserted-by":"publisher","first-page":"278","DOI":"10.1016\/j.pnmrs.2008.10.003","article-title":"Probing protein surface accessibility with solvent and paramagnetic molecules","volume":"54","author":"Bernini","year":"2009","journal-title":"Prog. Nucl. Mag. Res. Sp."},{"key":"B20","doi-asserted-by":"publisher","first-page":"1536","DOI":"10.1002\/cbic.200500124","article-title":"NMR spectroscopy of paramagnetic metalloproteins","volume":"6","author":"Bertini","year":"2005","journal-title":"Chembiochem"},{"key":"B21","doi-asserted-by":"publisher","first-page":"8090","DOI":"10.1021\/ja0396955","article-title":"Determination of protein structures consistent with NMR order parameters","volume":"126","author":"Best","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"B22","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/j.str.2005.09.012","article-title":"Structural interpretation of hydrogen exchange protection factors in proteins: characterization of the native state fluctuations of CI2","volume":"14","author":"Best","year":"2006","journal-title":"Structure"},{"key":"B23","doi-asserted-by":"publisher","first-page":"1638","DOI":"10.1126\/science.1130258","article-title":"The dynamic energy landscape of dihydrofolate reductase catalysis","volume":"313","author":"Boehr","year":"2006","journal-title":"Science"},{"key":"B24","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.sbi.2020.09.004","article-title":"How do intrinsically disordered protein regions encode a driving force for liquid\u2013liquid phase separation?","volume":"67","author":"Borcherds","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B25","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1038\/nature10349","article-title":"Solution structure of a minor and transiently formed state of a T4 lysozyme mutant","volume":"477","author":"Bouvignies","year":"2011","journal-title":"Nature"},{"key":"B26","doi-asserted-by":"publisher","first-page":"1767","DOI":"10.1038\/s41467-022-29408-z","article-title":"Temporal and spatial characterisation of protein liquid-liquid phase separation using NMR spectroscopy","volume":"13","author":"Bramham","year":"2022","journal-title":"Nat. Commun."},{"key":"B27","doi-asserted-by":"publisher","first-page":"1729","DOI":"10.1126\/science.1172046","article-title":"Germline P granules are liquid droplets that localize by controlled dissolution\/condensation","volume":"324","author":"Brangwynne","year":"2009","journal-title":"Science"},{"key":"B28","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.molcel.2015.09.006","article-title":"Residue-by-Residue view of in vitro FUS granules that bind the C-terminal domain of RNA polymerase II","volume":"60","author":"Burke","year":"2015","journal-title":"Mol. Cell"},{"key":"B29","doi-asserted-by":"publisher","first-page":"e2404457121","DOI":"10.1073\/pnas.2404457121","article-title":"An alpha-ketoglutarate conformational switch controls iron accessibility, activation, and substrate selection of the human FTO protein","volume":"121","author":"Burns","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B30","doi-asserted-by":"publisher","first-page":"9331","DOI":"10.1021\/acs.chemrev.1c01023","article-title":"NMR provides unique insight into the functional dynamics and interactions of intrinsically disordered proteins","volume":"122","author":"Camacho-Zarco","year":"2022","journal-title":"Chem. Rev."},{"key":"B31","doi-asserted-by":"publisher","first-page":"2224","DOI":"10.1021\/bi3001825","article-title":"Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts","volume":"51","author":"Camilloni","year":"2012","journal-title":"Biochemistry"},{"key":"B32","doi-asserted-by":"publisher","first-page":"9615","DOI":"10.1073\/pnas.0610313104","article-title":"Protein structure determination from NMR chemical shifts","volume":"104","author":"Cavalli","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B33","doi-asserted-by":"publisher","first-page":"094112","DOI":"10.1063\/1.4793625","article-title":"Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle","volume":"138","author":"Cavalli","year":"2013","journal-title":"J. Chem. Phys."},{"key":"B34","volume-title":"Protein NMR Spectroscopy: Principles and Practice","author":"Cavanagh","year":"2007"},{"key":"B35","doi-asserted-by":"publisher","first-page":"1175","DOI":"10.1107\/S1399004714005719","article-title":"Small angle X-Ray and neutron scattering from solutions of biological macromolecules","volume":"70","author":"Chavas","year":"2014","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"B36","doi-asserted-by":"publisher","first-page":"102334","DOI":"10.1016\/j.sbi.2022.102334","article-title":"Design and engineering of allosteric communications in proteins","volume":"73","author":"Chen","year":"2022","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B37","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1039\/b810232e","article-title":"Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement","volume":"4","author":"Clore","year":"2008","journal-title":"Mol. Biosyst."},{"key":"B38","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/S0167-7799(97)01135-9","article-title":"Determining the structures of large proteins and protein complexes by NMR","volume":"16","author":"Clore","year":"1998","journal-title":"Trends Biotechnol."},{"key":"B39","doi-asserted-by":"publisher","first-page":"4108","DOI":"10.1021\/cr900033p","article-title":"Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes","volume":"109","author":"Clore","year":"2009","journal-title":"Chem. Rev."},{"key":"B40","doi-asserted-by":"publisher","first-page":"2902","DOI":"10.1021\/ja028893d","article-title":"Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H\/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body\/torsion angle dynamics","volume":"125","author":"Clore","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"B41","doi-asserted-by":"publisher","first-page":"2923","DOI":"10.1021\/ja0386804","article-title":"How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?","volume":"126","author":"Clore","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"B42","doi-asserted-by":"publisher","first-page":"564","DOI":"10.1016\/s1367-5931(98)80084-7","article-title":"NMR structure determination of proteins and protein complexes larger than 20 kDa","volume":"2","author":"Clore","year":"","journal-title":"Curr. Opin. Chem. Biol."},{"key":"B43","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1006\/jmre.1997.1345","article-title":"Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude","volume":"131","author":"Clore","year":"","journal-title":"J. Magn. Reson"},{"key":"B44","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1016\/j.sbi.2007.08.013","article-title":"Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement","volume":"17","author":"Clore","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B45","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/bs.mie.2018.08.025","article-title":"The use of (13)C direct-detect NMR to characterize flexible and disordered proteins","volume":"611","author":"Cook","year":"2018","journal-title":"Methods Enzymol."},{"key":"B46","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1007\/BF00276625","article-title":"Allostery without conformational change. A plausible model","volume":"11","author":"Cooper","year":"1984","journal-title":"Eur. Biophys. J."},{"key":"B47","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1023\/a:1008392405740","article-title":"Protein backbone angle restraints from searching a database for chemical shift and sequence homology","volume":"13","author":"Cornilescu","year":"1999","journal-title":"J. Biomol. NMR"},{"key":"B48","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/j.pbiomolbio.2008.05.007","article-title":"Intrinsic disorder in scaffold proteins: getting more from less","volume":"98","author":"Cortese","year":"2008","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"B49","doi-asserted-by":"publisher","first-page":"13160","DOI":"10.1021\/jacs.5c22987","article-title":"Integrating NMR restraints into coarse-grained simulations: toward accurate conformational ensembles of complex protein systems","volume":"148","author":"Cullen","year":"2026","journal-title":"J. Am. Chem. Soc."},{"key":"B50","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1023\/a:1013302231549","article-title":"WaterLOGSY as a method for primary NMR screening: practical aspects and range of applicability","volume":"21","author":"Dalvit","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"B51","doi-asserted-by":"publisher","first-page":"7696","DOI":"10.1021\/ja034646d","article-title":"Fluorine-NMR experiments for high-throughput screening: theoretical aspects, practical considerations, and range of applicability","volume":"125","author":"Dalvit","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"B52","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1146\/annurev.bb.25.060196.001115","article-title":"Use of 19F NMR to probe protein structure and conformational changes","volume":"25","author":"Danielson","year":"1996","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"B53","doi-asserted-by":"publisher","first-page":"28795","DOI":"10.1073\/pnas.2008122117","article-title":"Comparative roles of charge, pi, and hydrophobic interactions in sequence-dependent phase separation of intrinsically disordered proteins","volume":"117","author":"Das","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B54","doi-asserted-by":"publisher","first-page":"e1005941","DOI":"10.1371\/journal.pcbi.1005941","article-title":"Sequence determinants of protein phase behavior from a coarse-grained model","volume":"14","author":"Dignon","year":"2018","journal-title":"PLoS Comput. Biol."},{"key":"B55","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1146\/annurev-physchem-071819-113553","article-title":"Biomolecular phase separation: from molecular driving forces to macroscopic properties","volume":"71","author":"Dignon","year":"2020","journal-title":"Annu. Rev. Phys. Chem."},{"key":"B56","doi-asserted-by":"publisher","first-page":"100091","DOI":"10.1016\/j.bbadva.2023.100091","article-title":"Applications of fluorescence spectroscopy in protein conformational changes and intermolecular contacts","volume":"3","author":"Dos Santos Rodrigues","year":"2023","journal-title":"BBA Adv."},{"key":"B57","doi-asserted-by":"publisher","first-page":"4481","DOI":"10.1016\/j.jmb.2020.05.024","article-title":"Hybrid thermophilic\/mesophilic enzymes reveal a role for conformational disorder in regulation of bacterial enzyme I","volume":"432","author":"Dotas","year":"2020","journal-title":"J. Mol. Biol."},{"key":"B58","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1038\/nrm1589","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"Dyson","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B59","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.sbi.2021.03.015","article-title":"NMR illuminates intrinsic disorder","volume":"70","author":"Dyson","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B60","doi-asserted-by":"publisher","first-page":"4702","DOI":"10.1021\/acs.analchem.9b00143","article-title":"(19)F dark-state exchange saturation transfer NMR reveals reversible formation of protein-specific large clusters in high-concentration protein mixtures","volume":"91","author":"Edwards","year":"2019","journal-title":"Anal. Chem."},{"key":"B61","doi-asserted-by":"publisher","first-page":"1520","DOI":"10.1126\/science.1066176","article-title":"Enzyme dynamics during catalysis","volume":"295","author":"Eisenmesser","year":"2002","journal-title":"Science"},{"key":"B62","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1038\/nature04105","article-title":"Intrinsic dynamics of an enzyme underlies catalysis","volume":"438","author":"Eisenmesser","year":"2005","journal-title":"Nature"},{"key":"B63","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1038\/s41589-021-00752-3","article-title":"NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation","volume":"17","author":"Emmanouilidis","year":"2021","journal-title":"Nat. Chem. Biol."},{"key":"B64","doi-asserted-by":"publisher","first-page":"4626","DOI":"10.1021\/ja906995x","article-title":"Refinement of ensembles describing unstructured proteins using NMR residual dipolar couplings","volume":"132","author":"Esteban-Martin","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"B65","doi-asserted-by":"publisher","first-page":"1379","DOI":"10.1073\/pnas.0909370107","article-title":"Mechanistic details of a protein-protein association pathway revealed by paramagnetic relaxation enhancement titration measurements","volume":"107","author":"Fawzi","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B66","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1038\/nature10577","article-title":"Atomic-resolution dynamics on the surface of amyloid-beta protofibrils probed by solution NMR","volume":"480","author":"Fawzi","year":"2011","journal-title":"Nature"},{"key":"B67","doi-asserted-by":"publisher","first-page":"1523","DOI":"10.1038\/nprot.2012.077","article-title":"Probing exchange kinetics and atomic resolution dynamics in high-molecular-weight complexes using dark-state exchange saturation transfer NMR spectroscopy","volume":"7","author":"Fawzi","year":"2012","journal-title":"Nat. Protoc."},{"key":"B68","doi-asserted-by":"publisher","first-page":"9468","DOI":"10.1021\/acs.chemrev.1c00871","article-title":"(13)C direct detected NMR for challenging systems","volume":"122","author":"Felli","year":"2022","journal-title":"Chem. Rev."},{"key":"B69","doi-asserted-by":"publisher","first-page":"102705","DOI":"10.1016\/j.sbi.2023.102705","article-title":"Protein disorder and autoinhibition: the role of multivalency and effective concentration","volume":"83","author":"Fenton","year":"2023","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B70","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1038\/nature19948","article-title":"Unravelling biological macromolecules with cryo-electron microscopy","volume":"537","author":"Fernandez-Leiro","year":"2016","journal-title":"Nature"},{"key":"B71","doi-asserted-by":"publisher","first-page":"801","DOI":"10.1038\/nmeth.3027","article-title":"Deep mutational scanning: a new style of protein science","volume":"11","author":"Fowler","year":"2014","journal-title":"Nat. Methods"},{"key":"B72","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1038\/nature05959","article-title":"Conformational entropy in molecular recognition by proteins","volume":"448","author":"Frederick","year":"2007","journal-title":"Nature"},{"key":"B73","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1146\/annurev.biophys.27.1.357","article-title":"The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins","volume":"27","author":"Gardner","year":"1998","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"B74","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1016\/j.str.2021.09.009","article-title":"Small, but powerful and attractive: (19)F in biomolecular NMR","volume":"30","author":"Gronenborn","year":"2022","journal-title":"Structure"},{"key":"B75","doi-asserted-by":"publisher","first-page":"e1004620","DOI":"10.1371\/journal.pcbi.1004620","article-title":"NMR methods to study dynamic allostery","volume":"12","author":"Grutsch","year":"2016","journal-title":"PLoS Comput. Biol."},{"key":"B76","doi-asserted-by":"publisher","first-page":"6503","DOI":"10.1021\/acs.chemrev.5b00590","article-title":"Protein allostery and conformational dynamics","volume":"116","author":"Guo","year":"2016","journal-title":"Chem. Rev."},{"key":"B77","doi-asserted-by":"publisher","first-page":"10548","DOI":"10.1021\/jacs.2c13647","article-title":"Liquid-Liquid phase separation modifies the dynamic properties of intrinsically disordered proteins","volume":"145","author":"Guseva","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"B78","doi-asserted-by":"publisher","first-page":"6264","DOI":"10.1073\/pnas.93.13.6264","article-title":"Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor","volume":"93","author":"Ha","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B79","doi-asserted-by":"publisher","first-page":"964","DOI":"10.1038\/nature06522","article-title":"Dynamic personalities of proteins","volume":"450","author":"Henzler-Wildman","year":"2007","journal-title":"Nature"},{"key":"B80","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1038\/nprot.2007.73","article-title":"Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry","volume":"2","author":"Hernandez","year":"2007","journal-title":"Nat. Protoc."},{"key":"B81","doi-asserted-by":"publisher","first-page":"3082","DOI":"10.1002\/cphc.201300219","article-title":"Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes","volume":"14","author":"Hocking","year":"2013","journal-title":"Chemphyschem"},{"key":"B82","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1146\/annurev-physchem-032511-143731","article-title":"Membrane protein structure and dynamics from NMR spectroscopy","volume":"63","author":"Hong","year":"2012","journal-title":"Annu. Rev. Phys. Chem."},{"key":"B83","doi-asserted-by":"publisher","first-page":"638","DOI":"10.1038\/384638a0","article-title":"NMR structure and mutagenesis of the Fas (APO-1\/CD95) death domain","volume":"384","author":"Huang","year":"1996","journal-title":"Nature"},{"key":"B84","doi-asserted-by":"publisher","first-page":"8583","DOI":"10.1021\/jacs.3c01003","article-title":"Environmentally ultrasensitive fluorine probe to resolve protein conformational ensembles by (19)F NMR and Cryo-EM","volume":"145","author":"Huang","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"B85","doi-asserted-by":"publisher","first-page":"725","DOI":"10.1016\/j.sbi.2013.06.008","article-title":"Technological advances in site-directed spin labeling of proteins","volume":"23","author":"Hubbell","year":"2013","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B86","doi-asserted-by":"publisher","first-page":"1541","DOI":"10.1021\/ja005590f","article-title":"Determination of protein backbone structure using only residual dipolar couplings","volume":"123","author":"Hus","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"B87","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1146\/annurev-cellbio-100913-013325","article-title":"Liquid-liquid phase separation in biology","volume":"30","author":"Hyman","year":"2014","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"B88","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1038\/nature04673","article-title":"Detecting transient intermediates in macromolecular binding by paramagnetic NMR","volume":"440","author":"Iwahara","year":"2006","journal-title":"Nature"},{"key":"B89","doi-asserted-by":"publisher","first-page":"5879","DOI":"10.1021\/ja031580d","article-title":"Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule","volume":"126","author":"Iwahara","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"B90","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/j.jmr.2006.10.003","article-title":"Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules","volume":"184","author":"Iwahara","year":"2007","journal-title":"J. Magn. Reson"},{"key":"B91","doi-asserted-by":"publisher","first-page":"1317","DOI":"10.1126\/science.aaw4951","article-title":"Protein condensates as aging Maxwell fluids","volume":"370","author":"Jawerth","year":"2020","journal-title":"Science"},{"key":"B92","doi-asserted-by":"publisher","first-page":"1270","DOI":"10.1021\/ja909973n","article-title":"Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts","volume":"132","author":"Jensen","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"B93","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1007\/978-1-0716-1197-5_5","article-title":"Isothermal titration calorimetry","volume":"2263","author":"Johnson","year":"2021","journal-title":"Methods Mol. Biol."},{"key":"B94","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"B95","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1038\/nsb0902-646","article-title":"Molecular dynamics simulations of biomolecules","volume":"9","author":"Karplus","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"B96","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1139\/bcb-76-2-3-145","article-title":"Protein dynamics from NMR","volume":"76","author":"Kay","year":"1998","journal-title":"Biochem. Cell Biol."},{"key":"B97","doi-asserted-by":"publisher","first-page":"662","DOI":"10.1038\/181662a0","article-title":"A three-dimensional model of the myoglobin molecule obtained by x-ray analysis","volume":"181","author":"Kendrew","year":"1958","journal-title":"Nature"},{"key":"B98","doi-asserted-by":"publisher","first-page":"748","DOI":"10.1016\/j.sbi.2003.10.008","article-title":"The role of dynamics in allosteric regulation","volume":"13","author":"Kern","year":"2003","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B99","doi-asserted-by":"publisher","first-page":"e2104897118","DOI":"10.1073\/pnas.2104897118","article-title":"Interaction hot spots for phase separation revealed by NMR studies of a CAPRIN1 condensed phase","volume":"118","author":"Kim","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B100","doi-asserted-by":"publisher","first-page":"1224","DOI":"10.1039\/c0cs00113a","article-title":"Hydrogen exchange mass spectrometry for studying protein structure and dynamics","volume":"40","author":"Konermann","year":"2011","journal-title":"Chem. Soc. Rev."},{"key":"B101","doi-asserted-by":"publisher","first-page":"10802","DOI":"10.3390\/molecules180910802","article-title":"Structural characterization of intrinsically disordered proteins by NMR spectroscopy","volume":"18","author":"Kosol","year":"2013","journal-title":"Molecules"},{"key":"B102","doi-asserted-by":"publisher","first-page":"2861","DOI":"10.1016\/j.jmb.2019.11.009","article-title":"Integrative modelling of biomolecular complexes","volume":"432","author":"Koukos","year":"2020","journal-title":"J. Mol. Biol."},{"key":"B103","doi-asserted-by":"publisher","first-page":"11504","DOI":"10.1073\/pnas.93.21.11504","article-title":"Structural studies of p21Waf1\/Cip1\/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity","volume":"93","author":"Kriwacki","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B104","doi-asserted-by":"publisher","first-page":"1443","DOI":"10.1126\/science.1251652","article-title":"Biochemistry. The resolution revolution","volume":"343","author":"Kuhlbrandt","year":"2014","journal-title":"Science"},{"key":"B105","doi-asserted-by":"publisher","first-page":"4421","DOI":"10.1021\/acs.biochem.8b00642","article-title":"NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations","volume":"57","author":"Leach","year":"2018","journal-title":"Biochemistry"},{"key":"B106","doi-asserted-by":"publisher","first-page":"1259","DOI":"10.1016\/j.str.2020.09.011","article-title":"Toward increased reliability, transparency, and accessibility in cross-linking mass spectrometry","volume":"28","author":"Leitner","year":"2020","journal-title":"Structure"},{"key":"B107","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1038\/nature10879","article-title":"Phase transitions in the assembly of multivalent signalling proteins","volume":"483","author":"Li","year":"2012","journal-title":"Nature"},{"key":"B108","doi-asserted-by":"publisher","first-page":"3787","DOI":"10.1021\/ja209931w","article-title":"Structure and dynamics of an unfolded protein examined by molecular dynamics simulation","volume":"134","author":"Lindorff-Larsen","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"B109","doi-asserted-by":"publisher","first-page":"444","DOI":"10.1038\/35073068","article-title":"Studying protein dynamics in living cells","volume":"2","author":"Lippincott-Schwartz","year":"2001","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B110","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1016\/bs.mie.2015.06.037","article-title":"Determining the secondary structure of membrane proteins and peptides via Electron Spin Echo Envelope Modulation (ESEEM) spectroscopy","volume":"564","author":"Liu","year":"2015","journal-title":"Methods Enzymol."},{"key":"B111","doi-asserted-by":"publisher","first-page":"8820","DOI":"10.1073\/pnas.1405011111","article-title":"Measuring hydrogen exchange rates in invisible protein excited states","volume":"111","author":"Long","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B112","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1042\/ETLS20190164","article-title":"Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof","volume":"4","author":"Martin","year":"2020","journal-title":"Emerg. Top. Life Sci."},{"key":"B113","doi-asserted-by":"publisher","first-page":"694","DOI":"10.1126\/science.aaw8653","article-title":"Valence and patterning of aromatic residues determine the phase behavior of prion-like domains","volume":"367","author":"Martin","year":"2020","journal-title":"Science"},{"key":"B114","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/bs.mie.2020.07.002","article-title":"Small-angle X-ray scattering experiments of monodisperse intrinsically disordered protein samples close to the solubility limit","volume":"646","author":"Martin","year":"2021","journal-title":"Methods Enzymol."},{"key":"B115","doi-asserted-by":"publisher","first-page":"1784","DOI":"10.1002\/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0.CO;2-Q","article-title":"Characterization of ligand binding by saturation transfer difference NMR spectroscopy","volume":"38","author":"Mayer","year":"1999","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"B116","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1016\/bs.mie.2015.06.035","article-title":"Hydrogen exchange mass spectrometry","volume":"566","author":"Mayne","year":"2016","journal-title":"Methods Enzymol."},{"key":"B117","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1146\/annurev.biophys.050708.133719","article-title":"Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR","volume":"38","author":"McDermott","year":"2009","journal-title":"Annu. Rev. Biophys."},{"key":"B118","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1146\/annurev-physchem-040214-121732","article-title":"Mass spectrometry of protein complexes: from origins to applications","volume":"66","author":"Mehmood","year":"2015","journal-title":"Annu. Rev. Phys. Chem."},{"key":"B119","doi-asserted-by":"publisher","first-page":"1506","DOI":"10.1021\/jacsau.2c00055","article-title":"Rheology and viscoelasticity of proteins and nucleic acids condensates","volume":"2","author":"Michieletto","year":"2022","journal-title":"JACS Au"},{"key":"B120","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1126\/science.1124964","article-title":"New tools provide new insights in NMR studies of protein dynamics","volume":"312","author":"Mittermaier","year":"2006","journal-title":"Science"},{"key":"B121","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1016\/s0022-2836(65)80285-6","article-title":"On the Nature of allosteric transitions: a plausible model","volume":"12","author":"Monod","year":"1965","journal-title":"J. Mol. Biol."},{"key":"B122","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1038\/nature13001","article-title":"The ensemble nature of allostery","volume":"508","author":"Motlagh","year":"2014","journal-title":"Nature"},{"key":"B123","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1016\/j.tcb.2011.04.008","article-title":"Atomic force microscopy: a nanoscopic window on the cell surface","volume":"21","author":"Muller","year":"2011","journal-title":"Trends Cell Biol."},{"key":"B124","doi-asserted-by":"publisher","first-page":"2375","DOI":"10.1074\/jbc.REV119.009847","article-title":"The (un)structural biology of biomolecular liquid-liquid phase separation using NMR spectroscopy","volume":"295","author":"Murthy","year":"2020","journal-title":"J. Biol. Chem."},{"key":"B125","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1038\/s41594-019-0250-x","article-title":"Molecular interactions underlying liquid-liquid phase separation of the FUS low-complexity domain","volume":"26","author":"Murthy","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B126","doi-asserted-by":"publisher","first-page":"100034","DOI":"10.1016\/j.yjsbx.2020.100034","article-title":"An allosteric pocket for inhibition of bacterial Enzyme I identified by NMR-based fragment screening","volume":"4","author":"Nguyen","year":"2020","journal-title":"J. Struct. Biol. X"},{"key":"B127","doi-asserted-by":"publisher","first-page":"2631","DOI":"10.1074\/jbc.RA117.001466","article-title":"The oligomerization state of bacterial enzyme I (EI) determines EI's allosteric stimulation or competitive inhibition by alpha-ketoglutarate","volume":"293","author":"Nguyen","year":"2018","journal-title":"J. Biol. Chem."},{"key":"B128","doi-asserted-by":"publisher","first-page":"4628","DOI":"10.1038\/s41467-025-59759-2","article-title":"LLPS REDIFINE allows the biophysical characterization of multicomponent condensates without tags or labels","volume":"16","author":"Novakovic","year":"2025","journal-title":"Nat. Commun."},{"key":"B129","doi-asserted-by":"publisher","first-page":"1000","DOI":"10.1038\/s41594-018-0147-0","article-title":"Cross-linking mass spectrometry: methods and applications in structural, molecular and systems biology","volume":"25","author":"O'Reilly","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B130","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1007\/s12551-017-0366-3","article-title":"Single-molecule fluorescence-based analysis of protein conformation, interaction, and oligomerization in cellular systems","volume":"10","author":"Okamoto","year":"2018","journal-title":"Biophys. Rev."},{"key":"B131","doi-asserted-by":"publisher","first-page":"16557","DOI":"10.1021\/jacs.3c03578","article-title":"Integrated NMR\/Molecular dynamics determination of the ensemble conformation of a thermodynamically stable CUUG RNA tetraloop","volume":"145","author":"Oxenfarth","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"B132","doi-asserted-by":"publisher","first-page":"3623","DOI":"10.1021\/cr030413t","article-title":"3rd, NMR characterization of the dynamics of biomacromolecules","volume":"104","author":"Palmer","year":"2004","journal-title":"Chem. Rev."},{"key":"B133","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1021\/ar500340a","article-title":"3rd, Enzyme dynamics from NMR spectroscopy","volume":"48","author":"Palmer","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"B134","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/bs.mie.2018.09.028","article-title":"Chemical exchange","volume":"615","author":"Palmer","year":"2019","journal-title":"Methods Enzymol."},{"key":"B135","doi-asserted-by":"publisher","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"B136","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.sbi.2019.09.007","article-title":"Molecular structure in biomolecular condensates","volume":"60","author":"Peran","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B137","doi-asserted-by":"publisher","first-page":"416","DOI":"10.1038\/185416a0","article-title":"Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis","volume":"185","author":"Perutz","year":"1960","journal-title":"Nature"},{"key":"B138","doi-asserted-by":"publisher","first-page":"12366","DOI":"10.1073\/pnas.94.23.12366","article-title":"Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution","volume":"94","author":"Pervushin","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B139","doi-asserted-by":"publisher","first-page":"206","DOI":"10.1021\/ar050087z","article-title":"NMR structure determination of protein-ligand complexes by lanthanide labeling","volume":"40","author":"Pintacuda","year":"2007","journal-title":"Acc. Chem. Res."},{"key":"B140","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1038\/nsmb1132","article-title":"Dynamically driven protein allostery","volume":"13","author":"Popovych","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B141","doi-asserted-by":"publisher","first-page":"6927","DOI":"10.1073\/pnas.0900595106","article-title":"Structural basis for cAMP-mediated allosteric control of the catabolite activator protein","volume":"106","author":"Popovych","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B142","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1016\/j.sbi.2003.09.012","article-title":"Exchange-transferred NOE spectroscopy and bound ligand structure determination","volume":"13","author":"Post","year":"2003","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B143","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1016\/bs.mie.2018.08.026","article-title":"Characterization of dynamic IDP complexes by NMR spectroscopy","volume":"611","author":"Prestel","year":"2018","journal-title":"Methods Enzymol."},{"key":"B144","doi-asserted-by":"publisher","first-page":"1895","DOI":"10.1016\/j.bpj.2018.10.004","article-title":"Active site breathing of Human Alkbh5 revealed by solution NMR and accelerated molecular dynamics","volume":"115","author":"Purslow","year":"2018","journal-title":"Biophys. J."},{"key":"B145","doi-asserted-by":"publisher","first-page":"9","DOI":"10.3389\/fmolb.2020.00009","article-title":"NMR methods for structural characterization of protein-protein complexes","volume":"7","author":"Purslow","year":"2020","journal-title":"Front. Mol. Biosci."},{"key":"B146","doi-asserted-by":"publisher","first-page":"eabi8215","DOI":"10.1126\/sciadv.abi8215","article-title":"N (6)-methyladenosine binding induces a metal-centered rearrangement that activates the human RNA demethylase Alkbh5","volume":"7","author":"Purslow","year":"2021","journal-title":"Sci. Adv."},{"key":"B147","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1017\/S0033583507004635","article-title":"X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution","volume":"40","author":"Putnam","year":"2007","journal-title":"Q. Rev. Biophys."},{"key":"B148","doi-asserted-by":"publisher","first-page":"10528","DOI":"10.1038\/s41467-025-65546-w","article-title":"Structural details of helix-mediated multimerization of the conserved region of TDP-43 C-terminal domain","volume":"16","author":"Rizuan","year":"2025","journal-title":"Nat. Commun."},{"key":"B149","doi-asserted-by":"publisher","first-page":"6365","DOI":"10.1021\/ja300265w","article-title":"3rd, Interpreting protein structural dynamics from NMR chemical shifts","volume":"134","author":"Robustelli","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"B150","doi-asserted-by":"publisher","first-page":"E4758","DOI":"10.1073\/pnas.1800690115","article-title":"Developing a molecular dynamics force field for both folded and disordered protein states","volume":"115","author":"Robustelli","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B151","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1146\/annurev-biochem-060713-035829","article-title":"Bringing dynamic molecular machines into focus by methyl-TROSY NMR","volume":"83","author":"Rosenzweig","year":"2014","journal-title":"Annu. Rev. Biochem."},{"key":"B152","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1007\/s10858-010-9401-4","article-title":"PCS-based structure determination of protein-protein complexes","volume":"46","author":"Saio","year":"2010","journal-title":"J. Biomol. NMR"},{"key":"B153","doi-asserted-by":"publisher","first-page":"13585","DOI":"10.1073\/pnas.95.23.13585","article-title":"TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins","volume":"95","author":"Salzmann","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B154","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1016\/j.jsb.2007.07.011","article-title":"Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography","volume":"160","author":"Sartori","year":"2007","journal-title":"J. Struct. Biol."},{"key":"B155","doi-asserted-by":"publisher","first-page":"1949","DOI":"10.1021\/ct800241d","article-title":"Direct comparison of experimental and calculated NMR scalar coupling constants for force field validation and adaptation","volume":"4","author":"Schmid","year":"2008","journal-title":"J. Chem. Theory Comput."},{"key":"B156","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.jmb.2011.12.056","article-title":"Protein structure determination from pseudocontact shifts using ROSETTA","volume":"416","author":"Schmitz","year":"2012","journal-title":"J. Mol. Biol."},{"key":"B157","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1146\/annurev.biophys.26.1.541","article-title":"Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules","volume":"26","author":"Schuck","year":"1997","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"B158","doi-asserted-by":"publisher","first-page":"13347","DOI":"10.1021\/jacs.3c03425","article-title":"Solution structure ensembles of the open and closed forms of the approximately 130 kDa enzyme I via AlphaFold modeling, coarse grained simulations, and NMR","volume":"145","author":"Sedinkin","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"B159","doi-asserted-by":"publisher","first-page":"168553","DOI":"10.1016\/j.jmb.2024.168553","article-title":"Elucidation of the mechanisms of inter-domain coupling in the monomeric State of enzyme I by high-pressure NMR","volume":"436","author":"Sedinkin","year":"2024","journal-title":"J. Mol. Biol."},{"key":"B160","doi-asserted-by":"publisher","first-page":"6133","DOI":"10.1073\/pnas.1017311108","article-title":"Mapping allostery through the covariance analysis of NMR chemical shifts","volume":"108","author":"Selvaratnam","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B161","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1126\/science.1187409","article-title":"Atomic-level characterization of the structural dynamics of proteins","volume":"330","author":"Shaw","year":"2010","journal-title":"Science"},{"key":"B162","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1007\/s10858-009-9333-z","article-title":"TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts","volume":"44","author":"Shen","year":"2009","journal-title":"J. Biomol. NMR"},{"key":"B163","doi-asserted-by":"publisher","first-page":"eaaf4382","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"B164","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1021\/acs.biochem.7b01031","article-title":"X-rays in the cryo-electron microscopy era: structural biology's dynamic future","volume":"57","author":"Shoemaker","year":"2018","journal-title":"Biochemistry"},{"key":"B165","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/j.jmr.2017.02.001","article-title":"Molecular dynamics simulations of NMR relaxation and diffusion of bulk hydrocarbons and water","volume":"277","author":"Singer","year":"2017","journal-title":"J. Magn. Reson"},{"key":"B166","doi-asserted-by":"publisher","first-page":"e62395","DOI":"10.3791\/62395","article-title":"15N CPMG relaxation dispersion for the investigation of protein conformational dynamics on the micros-ms timescale","volume":"170","author":"Singh","year":"2021","journal-title":"J. Vis. Exp."},{"key":"B167","doi-asserted-by":"publisher","first-page":"169575","DOI":"10.1016\/j.jmb.2025.169575","article-title":"Structure-based discovery of a non-competitive FTO inhibitor bound to a cryptic site at the domain interface","volume":"438","author":"Singh","year":"2026","journal-title":"J. Mol. Biol."},{"key":"B168","doi-asserted-by":"publisher","first-page":"102742","DOI":"10.1016\/j.sbi.2023.102742","article-title":"Multivalency emerges as a common feature of intrinsically disordered protein interactions","volume":"84","author":"Sipko","year":"2024","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B169","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.ymeth.2022.12.002","article-title":"Analysis of coordinated NMR chemical shifts to map allosteric regulatory networks in proteins","volume":"209","author":"Skeens","year":"2023","journal-title":"Methods"},{"key":"B170","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1007\/s10858-009-9362-7","article-title":"Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins","volume":"46","author":"Skrisovska","year":"2010","journal-title":"J. Biomol. NMR"},{"key":"B171","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1515\/BC.2010.093","article-title":"Small-angle X-ray and neutron scattering as a tool for structural systems biology","volume":"391","author":"Svergun","year":"2010","journal-title":"Biol. Chem."},{"key":"B172","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1038\/nature05201","article-title":"Visualization of transient encounter complexes in protein-protein association","volume":"444","author":"Tang","year":"2006","journal-title":"Nature"},{"key":"B173","doi-asserted-by":"publisher","first-page":"1078","DOI":"10.1038\/nature06232","article-title":"Open-to-closed transition in Apo maltose-binding protein observed by paramagnetic NMR","volume":"449","author":"Tang","year":"2007","journal-title":"Nature"},{"key":"B174","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/S0091-679X(07)84003-9","article-title":"Biosensor-surface plasmon resonance methods for quantitative analysis of biomolecular interactions","volume":"84","author":"Tanious","year":"2008","journal-title":"Methods Cell Biol."},{"key":"B175","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1016\/j.bpj.2019.08.030","article-title":"Quantifying dynamics in phase-separated condensates using fluorescence recovery after photobleaching","volume":"117","author":"Taylor","year":"2019","journal-title":"Biophys. J."},{"key":"B176","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1016\/j.ymeth.2019.05.015","article-title":"NMR characterization of RNA small molecule interactions","volume":"167","author":"Thompson","year":"2019","journal-title":"Methods"},{"key":"B177","doi-asserted-by":"publisher","first-page":"1111","DOI":"10.1126\/science.278.5340.1111","article-title":"Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium","volume":"278","author":"Tjandra","year":"1997","journal-title":"Science"},{"key":"B178","doi-asserted-by":"publisher","first-page":"332","DOI":"10.1016\/j.str.2012.12.013","article-title":"Structure and intrinsic disorder in protein autoinhibition","volume":"21","author":"Trudeau","year":"2013","journal-title":"Structure"},{"key":"B179","doi-asserted-by":"publisher","first-page":"10420","DOI":"10.1021\/ja030153x","article-title":"Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes","volume":"125","author":"Tugarinov","year":"","journal-title":"J. Am. Chem. Soc."},{"key":"B180","doi-asserted-by":"publisher","first-page":"13868","DOI":"10.1021\/ja030345s","article-title":"Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods","volume":"125","author":"Tugarinov","year":"","journal-title":"J. Am. Chem. Soc."},{"key":"B181","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1023\/B:JNMR.0000013824.93994.1f","article-title":"An isotope labeling strategy for methyl TROSY spectroscopy","volume":"28","author":"Tugarinov","year":"2004","journal-title":"J. Biomol. NMR"},{"key":"B182","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1038\/nprot.2006.101","article-title":"Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy","volume":"1","author":"Tugarinov","year":"2006","journal-title":"Nat. Protoc."},{"key":"B183","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1038\/nature08560","article-title":"Dynamic activation of an allosteric regulatory protein","volume":"462","author":"Tzeng","year":"2009","journal-title":"Nature"},{"key":"B184","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.sbi.2010.10.007","article-title":"Protein dynamics and allostery: an NMR view","volume":"21","author":"Tzeng","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B185","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1038\/nature11271","article-title":"Protein activity regulation by conformational entropy","volume":"488","author":"Tzeng","year":"2012","journal-title":"Nature"},{"key":"B186","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1007\/s10858-017-0099-4","article-title":"Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer","volume":"67","author":"Vallurupalli","year":"2017","journal-title":"J. Biomol. NMR"},{"key":"B187","doi-asserted-by":"publisher","first-page":"6589","DOI":"10.1021\/cr400525m","article-title":"Classification of intrinsically disordered regions and proteins","volume":"114","author":"van der Lee","year":"2014","journal-title":"Chem. Rev."},{"key":"B188","doi-asserted-by":"publisher","first-page":"26989","DOI":"10.1074\/jbc.M112.382291","article-title":"Conformational selection and substrate binding regulate the monomer\/dimer equilibrium of the C-terminal domain of Escherichia coli enzyme I","volume":"287","author":"Venditti","year":"2012","journal-title":"J. Biol. Chem."},{"key":"B189","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1007\/978-1-4939-7386-6_12","article-title":"Probing the atomic structure of transient protein contacts by paramagnetic relaxation enhancement solution NMR","volume":"1688","author":"Venditti","year":"2018","journal-title":"Methods Mol. Biol."},{"key":"B190","doi-asserted-by":"publisher","first-page":"e20","DOI":"10.1093\/nar\/gkm1062","article-title":"Measuring the dynamic surface accessibility of RNA with the small paramagnetic molecule TEMPOL","volume":"36","author":"Venditti","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"B191","doi-asserted-by":"publisher","first-page":"894","DOI":"10.1016\/j.jmb.2009.07.003","article-title":"Minimum-energy path for a u6 RNA conformational change involving protonation, base-pair rearrangement and base flipping","volume":"391","author":"Venditti","year":"2009","journal-title":"J. Mol. Biol."},{"key":"B192","doi-asserted-by":"publisher","first-page":"5960","DOI":"10.1038\/ncomms6960","article-title":"Large interdomain rearrangement triggered by suppression of micro-to millisecond dynamics in bacterial Enzyme I","volume":"6","author":"Venditti","year":"","journal-title":"Nat. Commun."},{"key":"B193","doi-asserted-by":"publisher","first-page":"11565","DOI":"10.1073\/pnas.1515366112","article-title":"Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering","volume":"112","author":"Venditti","year":"","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B194","doi-asserted-by":"publisher","first-page":"6305","DOI":"10.1021\/acs.chemrev.5b00592","article-title":"Hybrid approaches to structural characterization of conformational ensembles of complex macromolecular systems combining NMR residual dipolar couplings and solution X-ray scattering","volume":"116","author":"Venditti","year":"2016","journal-title":"Chem. Rev."},{"key":"B195","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1107\/S2053230X17003740","article-title":"Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery","volume":"73","author":"Venien-Bryan","year":"2017","journal-title":"Acta Crystallogr. F. Struct. Biol. Commun."},{"key":"B196","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1016\/j.cell.2018.06.006","article-title":"A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins","volume":"174","author":"Wang","year":"2018","journal-title":"Cell"},{"key":"B197","doi-asserted-by":"publisher","first-page":"913","DOI":"10.1126\/science.1228565","article-title":"Biochemistry. Integrative structural biology","volume":"339","author":"Ward","year":"2013","journal-title":"Science"},{"key":"B198","doi-asserted-by":"publisher","first-page":"24826","DOI":"10.1038\/srep24826","article-title":"Two-dimensional NMR lineshape analysis","volume":"6","author":"Waudby","year":"2016","journal-title":"Sci. Rep."},{"key":"B199","doi-asserted-by":"publisher","first-page":"e202402820","DOI":"10.1002\/chem.202402820","article-title":"Fluorine labeling and (19)F NMR spectroscopy to study biological molecules and molecular complexes","volume":"31","author":"Werle","year":"2025","journal-title":"Chemistry"},{"key":"B200","doi-asserted-by":"publisher","first-page":"16424","DOI":"10.1021\/bi991765q","article-title":"Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques","volume":"38","author":"Wilkins","year":"1999","journal-title":"Biochemistry"},{"key":"B201","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pnmrs.2013.02.001","article-title":"Using chemical shift perturbation to characterise ligand binding","volume":"73","author":"Williamson","year":"2013","journal-title":"Prog. Nucl. Magn. Reson Spectrosc."},{"key":"B202","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1007\/BF00175245","article-title":"The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data","volume":"4","author":"Wishart","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"B203","doi-asserted-by":"publisher","first-page":"566","DOI":"10.1016\/j.str.2019.01.003","article-title":"Allostery in its many disguises: from theory to applications","volume":"27","author":"Wodak","year":"2019","journal-title":"Structure"},{"key":"B204","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1006\/jmbi.1999.3110","article-title":"Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm","volume":"293","author":"Wright","year":"1999","journal-title":"J. Mol. Biol."},{"key":"B205","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1038\/nrm3920","article-title":"Intrinsically disordered proteins in cellular signalling and regulation","volume":"16","author":"Wright","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B206","doi-asserted-by":"publisher","first-page":"923","DOI":"10.1038\/nsb1101-923","article-title":"The way to NMR structures of proteins","volume":"8","author":"Wuthrich","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"B207","doi-asserted-by":"publisher","first-page":"3340","DOI":"10.1002\/anie.200300595","article-title":"NMR studies of structure and function of biological macromolecules (Nobel lecture)","volume":"42","author":"Wuthrich","year":"2003","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"B208","doi-asserted-by":"publisher","first-page":"2115","DOI":"10.1021\/jacs.7b09576","article-title":"Probing conformational exchange in weakly interacting, slowly exchanging protein systems via off-resonance R(1rho) experiments: application to studies of protein phase separation","volume":"140","author":"Yuwen","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"B209","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1021\/bi011870b","article-title":"Mapping protein-protein interactions in solution by NMR spectroscopy","volume":"41","author":"Zuiderweg","year":"2002","journal-title":"Biochemistry"},{"key":"B210","doi-asserted-by":"publisher","first-page":"1274","DOI":"10.1002\/pro.4135","article-title":"Introduction: biophysics of biomolecular condensates","volume":"30","author":"Zweckstetter","year":"2021","journal-title":"Protein Sci."}],"container-title":["Frontiers in Molecular Biosciences"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2026.1941622\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T08:55:21Z","timestamp":1789116921000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2026.1941622\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,11]]},"references-count":210,"alternative-id":["10.3389\/fmolb.2026.1941622"],"URL":"https:\/\/doi.org\/10.3389\/fmolb.2026.1941622","relation":{},"ISSN":["2296-889X"],"issn-type":[{"value":"2296-889X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,11]]},"article-number":"1941622"}}