{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T18:49:04Z","timestamp":1792003744414,"version":"4.4.0"},"reference-count":74,"publisher":"American Chemical Society (ACS)","issue":"40","license":[{"start":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T00:00:00Z","timestamp":1790899200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001711","name":"Schweizerischer Nationalfonds zur F?rderung der Wissenschaftlichen Forschung","doi-asserted-by":"publisher","award":["207755"],"award-info":[{"award-number":["207755"]}],"id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,14]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Protein dynamics are central to their folding and function, yet the sparsely populated conformational states that underpin these processes remain difficult to characterize at atomic resolution. Chemical exchange saturation transfer (CEST) NMR can detect such states and is particularly sensitive to rapid exchange between two minor conformations. This \u201cminor-state exchange\u201d, however, broadens and displaces the minor-state dip in CEST profiles, leading to parameter degeneracy that can preclude quantitative reconstruction of multistate exchange networks. Here, we show that, in the presence of rapid \u201cminor-exchange\u201d, the apparent minor-state chemical shift obtained from two-state fits varies systematically with the static magnetic field, B0. We exploit this field dependence to develop a nonperturbative, multi-field CEST strategy that distinguishes otherwise degenerate exchange models. Applying multi-field 15N-CEST to the model protein Im7 revealed a folding intermediate populated at \u223c1% that exchanges with the folded state on a \u223c2 ms time scale and with an unfolded state populated at \u223c0.4% on a \u223c200 \u03bcs time scale. Although the unfolded state does not produce a separate CEST dip, its exchange is encoded in the line width and B0-dependent position of the intermediate-state dip. Analysis of the 15N-CEST data provides populations, microscopic exchange rates, and residue-specific 15N chemical shifts for all three states. The resulting Im7 free-energy landscape is sequential, with folding proceeding through the intermediate and no detectable direct exchange between the folded and unfolded states. Multi-field CEST provides a broadly applicable, perturbation-free approach for resolving biomolecular dynamics at equilibrium.<\/jats:p>","DOI":"10.1021\/jacs.6c16569","type":"journal-article","created":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T09:01:35Z","timestamp":1790931695000},"page":"43873-43882","source":"Crossref","is-referenced-by-count":0,"title":["Multi-Field\nCEST NMR Reconstructs a Protein Folding\nLandscape"],"prefix":"10.1021","volume":"148","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2738-0376","authenticated-orcid":true,"given":"Ved Prakash","family":"Tiwari","sequence":"first","affiliation":[{"name":"Biozentrum, University of Basel , Klingelbergstrasse 70 , ,","place":["Basel, Switzerland, 4056"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laetitia","family":"Roz\u030cic\u0301","sequence":"additional","affiliation":[{"name":"Biozentrum, University of Basel , Klingelbergstrasse 70 , ,","place":["Basel, Switzerland, 4056"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6709-4684","authenticated-orcid":true,"given":"Sebastian","family":"Hiller","sequence":"additional","affiliation":[{"name":"Biozentrum, University of Basel , Klingelbergstrasse 70 , ,","place":["Basel, Switzerland, 4056"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,2]]},"reference":[{"issue":"7172","key":"2026101414094633200_cit1","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"},{"issue":"11","key":"2026101414094633200_cit2","doi-asserted-by":"publisher","first-page":"789","DOI":"10.1038\/nchembio.232","article-title":"The Role\nof Dynamic Conformational\nEnsembles in Biomolecular Recognition","volume":"5","author":"Boehr","year":"2009","journal-title":"Nat.\nChem. Biol."},{"issue":"11","key":"2026101414094633200_cit3","doi-asserted-by":"publisher","first-page":"808","DOI":"10.1038\/nchembio.238","article-title":"NMR Spectroscopy Brings Invisible Protein States into\nFocus","volume":"5","author":"Baldwin","year":"2009","journal-title":"Nat. Chem. Biol."},{"issue":"3","key":"2026101414094633200_cit4","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1002\/prot.340210302","article-title":"Funnels, Pathways,\nand the Energy Landscape of Protein Folding: A Synthesis","volume":"21","author":"Bryngelson","year":"1995","journal-title":"Proteins: struct., Funct., Bioinf."},{"issue":"6110","key":"2026101414094633200_cit5","doi-asserted-by":"publisher","first-page":"1042","DOI":"10.1126\/science.1219021","article-title":"The Protein-Folding\nProblem, 50 Years On","volume":"338","author":"Dill","year":"2012","journal-title":"Science"},{"key":"2026101414094633200_cit6","volume-title":"Protein Actions: principles\nand Modeling","author":"Bahar","year":"2017"},{"issue":"7064","key":"2026101414094633200_cit7","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1038\/nature04105","article-title":"Intrinsic\nDynamics of an Enzyme Underlies Catalysis","volume":"438","author":"Eisenmesser","year":"2005","journal-title":"Nature"},{"issue":"5793","key":"2026101414094633200_cit8","doi-asserted-by":"publisher","first-page":"1638","DOI":"10.1126\/science.1130258","article-title":"The Dynamic Energy\nLandscape of Dihydrofolate Reductase Catalysis","volume":"313","author":"Boehr","year":"2006","journal-title":"Science"},{"issue":"6999","key":"2026101414094633200_cit9","doi-asserted-by":"publisher","first-page":"586","DOI":"10.1038\/nature02655","article-title":"Low-Populated Folding Intermediates\nof Fyn SH3 Characterized by Relaxation Dispersion NMR","volume":"430","author":"Korzhnev","year":"2004","journal-title":"Nature"},{"issue":"6079","key":"2026101414094633200_cit10","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1126\/science.1214203","article-title":"Structure of an Intermediate State in Protein Folding\nand Aggregation","volume":"336","author":"Neudecker","year":"2012","journal-title":"Science"},{"issue":"6513","key":"2026101414094633200_cit11","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1126\/science.abc2754","article-title":"Conformational\nStates Dynamically Populated by a Kinase Determine Its Function","volume":"370","author":"Xie","year":"2020","journal-title":"Science"},{"issue":"6","key":"2026101414094633200_cit12","doi-asserted-by":"publisher","first-page":"810","DOI":"10.1016\/j.str.2018.03.018","article-title":"K-Ras Populates Conformational\nStates Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D","volume":"26","author":"Parker","year":"2018","journal-title":"Structure"},{"issue":"21","key":"2026101414094633200_cit13","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2426632122","article-title":"Activation\nDynamics of Ubiquitin-Specific Protease\n7","volume":"122","author":"Valles","year":"2025","journal-title":"Proc. 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A."},{"issue":"4","key":"2026101414094633200_cit23","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1007\/s10858-017-0099-4","article-title":"Probing Conformational\nDynamics in Biomolecules via Chemical Exchange Saturation Transfer:\nA Primer","volume":"67","author":"Vallurupalli","year":"2017","journal-title":"J. Biomol. NMR"},{"issue":"46","key":"2026101414094633200_cit24","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2115113118","article-title":"The A39G FF\nDomain Folds on a Volcano-Shaped Free Energy Surface via Separate\nPathways","volume":"118","author":"Tiwari","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026101414094633200_cit25","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/j.sbi.2019.10.008","article-title":"Unveiling Invisible Protein States with NMR Spectroscopy","volume":"60","author":"Alderson","year":"2020","journal-title":"Curr. Opin. Struct. 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Soc."},{"key":"2026101414094633200_cit32","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1007\/s10858-006-0001-2","article-title":"Assessment\nof the Effects of Increased\nRelaxation Dispersion Data on the Extraction of 3-Site Exchange Parameters\nCharacterizing the Unfolding of an SH3 Domain","volume":"34","author":"Neudecker","year":"2006","journal-title":"J. Biomol. NMR"},{"issue":"10","key":"2026101414094633200_cit33","doi-asserted-by":"publisher","first-page":"2687","DOI":"10.1002\/anie.201713172","article-title":"Targeting\na Dark\nExcited State of HIV-1 Nucleocapsid by Antiretroviral Thioesters Revealed\nby NMR Spectroscopy","volume":"57","author":"Deshmukh","year":"2018","journal-title":"Angew. Chem., Int. Ed."},{"issue":"15","key":"2026101414094633200_cit34","doi-asserted-by":"publisher","first-page":"4156","DOI":"10.1002\/anie.201209118","article-title":"Probing Slow Chemical Exchange at Carbonyl Sites in\nProteins by Chemical Exchange Saturation Transfer NMR Spectroscopy","volume":"52","author":"Vallurupalli","year":"2013","journal-title":"Angew. Chem., Int. Ed."},{"issue":"11","key":"2026101414094633200_cit35","doi-asserted-by":"publisher","first-page":"2892","DOI":"10.1063\/1.1734121","article-title":"Study of Moderately\nRapid Chemical Exchange Reactions\nby Means of Nuclear Magnetic Double Resonance","volume":"39","author":"Forse\u0301n","year":"1963","journal-title":"J. Chem. Phys."},{"issue":"4","key":"2026101414094633200_cit36","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1006\/jmbi.2001.5001","article-title":"Acidic Conditions\nStabilise Intermediates Populated during the Folding of Im7 and Im9","volume":"312","author":"Gorski","year":"2001","journal-title":"J. Mol. Biol."},{"issue":"5","key":"2026101414094633200_cit37","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1212222110","article-title":"High-Pressure NMR Reveals\nClose Similarity between Cold and Alcohol Protein Denaturation in\nUbiquitin","volume":"110","author":"Vajpai","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"50","key":"2026101414094633200_cit38","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2416682121","article-title":"Mapping the FF Domain Folding Pathway\nvia Structures of Transiently Populated Folding Intermediates","volume":"121","author":"De","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026101414094633200_cit39","doi-asserted-by":"publisher","first-page":"RP93562","DOI":"10.7554\/eLife.93562.4","article-title":"On the pH-Dependence\nof \u03b1-Synuclein\nAmyloid Polymorphism and the Role of Secondary Nucleation in Seed-Based\nAmyloid Propagation","volume":"12","author":"Frey","year":"2024","journal-title":"Elife"},{"issue":"21","key":"2026101414094633200_cit40","doi-asserted-by":"publisher","first-page":"7671","DOI":"10.1073\/pnas.1315346111","article-title":"Solution Conditions\nDetermine the Relative Importance of Nucleation and Growth Processes\nin \u03b1-Synuclein Aggregation","volume":"111","author":"Buell","year":"2014","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"issue":"20","key":"2026101414094633200_cit41","doi-asserted-by":"publisher","first-page":"6470","DOI":"10.1021\/bi952501g","article-title":"The Acid-Mediated Denaturation Pathway\nof Transthyretin Yields a Conformational Intermediate That Can Self-Assemble\ninto Amyloid","volume":"35","author":"Lai","year":"1996","journal-title":"Biochemistry"},{"issue":"7","key":"2026101414094633200_cit42","doi-asserted-by":"publisher","first-page":"2311","DOI":"10.1021\/bi052434i","article-title":"A Systematic\nStudy of the Effect\nof Physiological Factors on \u03922-Microglobulin Amyloid Formation\nat Neutral pH","volume":"45","author":"Myers","year":"2006","journal-title":"Biochemistry"},{"issue":"3","key":"2026101414094633200_cit43","doi-asserted-by":"publisher","first-page":"209","DOI":"10.1038\/nsb757","article-title":"Im7 Folding Mechanism: Misfolding\non a Path to the Native State","volume":"9","author":"Capaldi","year":"2002","journal-title":"Nat. Struct.\nBiol."},{"issue":"3","key":"2026101414094633200_cit44","doi-asserted-by":"publisher","first-page":"1001","DOI":"10.1016\/j.jmb.2006.11.012","article-title":"NMR Analysis of the Conformational Properties of the\nTrapped On-Pathway Folding Intermediate of the Bacterial Immunity\nProtein Im7","volume":"366","author":"Whittaker","year":"2007","journal-title":"J. Mol. Biol."},{"issue":"4","key":"2026101414094633200_cit45","doi-asserted-by":"publisher","first-page":"511","DOI":"10.1016\/j.jmb.2011.09.038","article-title":"NMR Characterisation\nof the Relationship\nbetween Frustration and the Excited State of Im7","volume":"414","author":"Whittaker","year":"2011","journal-title":"J. Mol. Biol."},{"issue":"1","key":"2026101414094633200_cit46","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/j.jmb.2004.01.004","article-title":"Equilibrium Hydrogen\nExchange Reveals\nExtensive Hydrogen Bonded Secondary Structure in the On-Pathway Intermediate\nof Im7","volume":"337","author":"Gorski","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"6","key":"2026101414094633200_cit47","doi-asserted-by":"publisher","first-page":"3178","DOI":"10.1021\/ja210711v","article-title":"Quantifying Millisecond\nExchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using\nSide-Chain 1H Probes","volume":"134","author":"Hansen","year":"2012","journal-title":"J. Am. Chem. Soc."},{"issue":"3","key":"2026101414094633200_cit48","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1007\/s10858-013-9711-4","article-title":"Probing Slowly Exchanging Protein\nSystems via 13C \u03b1-CEST: Monitoring Folding of the Im7 Protein","volume":"55","author":"Hansen","year":"2013","journal-title":"J. Biomol. NMR"},{"issue":"11","key":"2026101414094633200_cit49","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.1601625","article-title":"A Molecular Mechanism\nof Chaperone-Client Recognition","volume":"2","author":"He","year":"2016","journal-title":"Sci. Adv."},{"issue":"3","key":"2026101414094633200_cit50","doi-asserted-by":"publisher","first-page":"430","DOI":"10.1063\/1.1744152","article-title":"Reaction\nRates by Nuclear Magnetic Resonance","volume":"28","author":"McConnell","year":"1958","journal-title":"J. Chem.\nPhys."},{"key":"2026101414094633200_cit51","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-164491-8.X5000-3","volume-title":"Protein NMR Spectroscopy:\nprinciples and Practice","author":"Cavanagh","year":"2007","edition":"2nd"},{"issue":"3","key":"2026101414094633200_cit52","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/0022-2364(78)90048-3","article-title":"Limiting Equations\nfor Exchange Broadening in Two-Site\nNMR Systems with Very Unequal Populations","volume":"32","author":"Anet","year":"1978","journal-title":"J.\nMagn. Reson"},{"issue":"41","key":"2026101414094633200_cit53","doi-asserted-by":"publisher","first-page":"12352","DOI":"10.1021\/ja0207089","article-title":"Reconstructing NMR\nSpectra of \u201cInvisible\u201d\nExcited Protein States Using HSQC and HMQC Experiments","volume":"124","author":"Skrynnikov","year":"2002","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026101414094633200_cit54","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1016\/j.jmr.2004.06.005","article-title":"Theoretical Study of R1\u03c1 Rotating-Frame\nand R2 Free-Precession Relaxation in the Presence of n-Site Chemical\nExchange","volume":"170","author":"Trott","year":"2004","journal-title":"J. Magn. Reson."},{"issue":"5\u20136","key":"2026101414094633200_cit55","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1007\/s10858-022-00403-2","article-title":"Optimizing\nFrequency Sampling in\nCEST Experiments","volume":"76","author":"Bolik-Coulon","year":"2022","journal-title":"J. Biomol. NMR"},{"issue":"20","key":"2026101414094633200_cit56","doi-asserted-by":"publisher","first-page":"13794","DOI":"10.1039\/C6CP01127F","article-title":"Determination of Pseudocontact\nShifts of Low-Populated Excited States by NMR Chemical Exchange Saturation\nTransfer","volume":"18","author":"Ma","year":"2016","journal-title":"Phys. Chem. Chem. Phys."},{"issue":"1","key":"2026101414094633200_cit57","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1038\/83074","article-title":"Ultrarapid\nMixing Experiments Reveal That Im7 Folds via an On-Pathway Intermediate","volume":"8","author":"Capaldi","year":"2001","journal-title":"Nat. Struct. Biol."},{"issue":"17","key":"2026101414094633200_cit58","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1400577111","article-title":"Measurement of Histidine\npKa Values and Tautomer Populations\nin Invisible Protein States","volume":"111","author":"Hansen","year":"2014","journal-title":"Proc. Natl. Acad.\nSci. U. S. A."},{"issue":"1","key":"2026101414094633200_cit59","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1016\/j.jmb.2004.05.049","article-title":"Trapping the On-Pathway Folding Intermediate\nof Im7 at Equilibrium","volume":"341","author":"Spence","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"50","key":"2026101414094633200_cit60","doi-asserted-by":"publisher","first-page":"19825","DOI":"10.1073\/pnas.0709922104","article-title":"Consequences\nof Localized Frustration for the Folding Mechanism of the IM7 Protein","volume":"104","author":"Sutto","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"3","key":"2026101414094633200_cit61","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1038\/nsmb.1562","article-title":"The Mechanism\nof Folding of Im7 Reveals Competition between Functional and Kinetic\nEvolutionary Constraints","volume":"16","author":"Friel","year":"2009","journal-title":"Nat. Struct. 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