{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T01:25:32Z","timestamp":1794273932277,"version":"4.9.0"},"reference-count":63,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,7,10]],"date-time":"2026-07-10T00:00:00Z","timestamp":1783641600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001663","name":"VolkswagenStiftung","doi-asserted-by":"publisher","award":["76251-4659\/2022 ( ZN 4042 )"],"award-info":[{"award-number":["76251-4659\/2022 ( ZN 4042 )"]}],"id":[{"id":"10.13039\/501100001663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","award":["101141570"],"award-info":[{"award-number":["101141570"]}],"id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100018694","name":"European Commission Marie Sklodowska-Curie Actions","doi-asserted-by":"publisher","award":["101148056"],"award-info":[{"award-number":["101148056"]}],"id":[{"id":"10.13039\/100018694","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100018693","name":"HORIZON EUROPE Framework Programme","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100018693","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Structural Biology"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.sbi.2026.103340","type":"journal-article","created":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T08:49:57Z","timestamp":1784537397000},"page":"103340","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Nuclear magnetic resonance spectroscopy as a tool to probe molecular condensates"],"prefix":"10.1016","volume":"100","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3748-2731","authenticated-orcid":false,"given":"Gonzalo","family":"P\u00e9rez-Mej\u00edas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2536-6581","authenticated-orcid":false,"given":"Markus","family":"Zweckstetter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.sbi.2026.103340_bib1","doi-asserted-by":"crossref","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":"10.1016\/j.sbi.2026.103340_bib2","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.tibs.2021.01.002","article-title":"Biomolecular condensates and their links to cancer progression","volume":"46","author":"Cai","year":"2021","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.sbi.2026.103340_bib3","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1146\/annurev-genet-112618-043527","article-title":"Liquid\u2013liquid phase separation in disease","volume":"53","author":"Alberti","year":"2019","journal-title":"Annu Rev Genet"},{"key":"10.1016\/j.sbi.2026.103340_sref4","doi-asserted-by":"crossref","first-page":"7730","DOI":"10.1038\/s41467-025-62055-8","article-title":"Current practices in the study of biomolecular condensates: a community comment","volume":"16","author":"Alberti","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103340_bib5","first-page":"89","article-title":"Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro","volume":"27","author":"D\u00f6rner","year":"2025","journal-title":"EMBO Rep"},{"key":"10.1016\/j.sbi.2026.103340_bib6","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202218078","article-title":"Determining the physico-chemical composition of biomolecular condensates from spatially-resolved NMR","author":"Pantoja","year":"2023","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.sbi.2026.103340_bib7","doi-asserted-by":"crossref","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":"10.1016\/j.sbi.2026.103340_sref8","series-title":"LLPS REDIFINE allows the biophysical characterization of multicomponent condensates without tags or labels","author":"Novakovic","year":"2024"},{"key":"10.1016\/j.sbi.2026.103340_bib9","doi-asserted-by":"crossref","first-page":"1785","DOI":"10.1038\/s41557-025-01968-9","article-title":"Water-detected NMR allows dynamic observations of repeat-expansion RNA condensates","volume":"17","author":"Schmoll","year":"2025","journal-title":"Nat Chem"},{"key":"10.1016\/j.sbi.2026.103340_bib10","series-title":"Selective ion binding and uptake shape the microenvironment of biomolecular condensates","author":"Smokers","year":"2024"},{"key":"10.1016\/j.sbi.2026.103340_bib11","doi-asserted-by":"crossref","first-page":"47237","DOI":"10.1021\/jacs.5c14476","article-title":"Multiplexed analysis of multicomponent biomolecular condensates without any tag","volume":"147","author":"P\u00e1lfy","year":"2025","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2026.103340_bib12","doi-asserted-by":"crossref","DOI":"10.1002\/cbic.202500401","article-title":"Quantification of small molecule partitioning in a biomolecular condensate with 2D nuclear magnetic resonance spectroscopy","volume":"26","author":"Buhl","year":"2025","journal-title":"Chembiochem"},{"key":"10.1016\/j.sbi.2026.103340_bib13","doi-asserted-by":"crossref","first-page":"5892","DOI":"10.1038\/s41467-023-41586-y","article-title":"Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain","volume":"14","author":"Mukherjee","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103340_bib14","doi-asserted-by":"crossref","first-page":"7724","DOI":"10.1021\/acs.jpclett.4c01153","article-title":"Hydrogen-bonded network of water in phase-separated biomolecular condensates","volume":"15","author":"Joshi","year":"2024","journal-title":"J Phys Chem Lett"},{"key":"10.1016\/j.sbi.2026.103340_bib15","doi-asserted-by":"crossref","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":"10.1016\/j.sbi.2026.103340_bib16","doi-asserted-by":"crossref","first-page":"6719","DOI":"10.1021\/acs.chemrev.1c00774","article-title":"Conformational dynamics of intrinsically disordered proteins regulate biomolecular condensate chemistry","volume":"122","author":"Abyzov","year":"2022","journal-title":"Chem Rev"},{"key":"10.1016\/j.sbi.2026.103340_bib17","doi-asserted-by":"crossref","first-page":"E8194","DOI":"10.1073\/pnas.1706197114","article-title":"Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation","volume":"114","author":"Brady","year":"2017","journal-title":"Proc Natl Acad Sci"},{"key":"10.1016\/j.sbi.2026.103340_bib18","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1126\/science.aax4240","article-title":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation","volume":"365","author":"Kim","year":"2019","journal-title":"Science"},{"key":"10.1016\/j.sbi.2026.103340_bib19","doi-asserted-by":"crossref","first-page":"2471","DOI":"10.1021\/jacs.9b12208","article-title":"NMR experiments for studies of dilute and condensed protein phases: application to the phase-separating protein CAPRIN1","volume":"142","author":"Wong","year":"2020","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2026.103340_bib20","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"},{"key":"10.1016\/j.sbi.2026.103340_bib21","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2210492119","article-title":"Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory","volume":"119","author":"Toyama","year":"2022","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.sbi.2026.103340_bib22","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102776","article-title":"Surface electrostatics dictate RNA-binding protein CAPRIN1 condensate concentration and hydrodynamic properties","volume":"299","author":"Toyama","year":"2023","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2026.103340_bib23","doi-asserted-by":"crossref","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":"10.1016\/j.sbi.2026.103340_bib24","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.molcel.2017.12.022","article-title":"Mechanistic view of hnRNPA2 low-complexity domain structure, interactions, and phase separation altered by mutation and arginine methylation","volume":"69","author":"Ryan","year":"2018","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2026.103340_bib25","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/s41594-019-0250-x","article-title":"Molecular interactions underlying liquid\u2212liquid phase separation of the FUS low-complexity domain","volume":"26","author":"Murthy","year":"2019","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib26","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1038\/s41594-021-00677-4","article-title":"Molecular interactions contributing to FUS SYGQ LC-RGG phase separation and co-partitioning with RNA polymerase II heptads","volume":"28","author":"Murthy","year":"2021","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib27","doi-asserted-by":"crossref","first-page":"8071","DOI":"10.1021\/jacs.3c12034","article-title":"Insights into molecular diversity within the FUS\/EWS\/TAF15 protein family: unraveling phase separation of the N-Terminal low-complexity domain from RNA-binding protein EWS","volume":"146","author":"Johnson","year":"2024","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2026.103340_sref28","doi-asserted-by":"crossref","first-page":"1076","DOI":"10.1038\/s41589-024-01828-6","article-title":"Expanding the molecular grammar of polar residues and arginine in FUS phase separation","volume":"21","author":"Wake","year":"2025","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib29","doi-asserted-by":"crossref","first-page":"gkaf664","DOI":"10.1093\/nar\/gkaf664","article-title":"Molecular mechanisms of biomolecular condensate formation in Drosophila melanogaster siRNA biogenesis","volume":"53","author":"Hipp","year":"2025","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.sbi.2026.103340_bib30","doi-asserted-by":"crossref","first-page":"5979","DOI":"10.1038\/s41467-023-41633-8","article-title":"Driving forces behind phase separation of the carboxy-terminal domain of RNA polymerase II","volume":"14","author":"Flores-Solis","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103340_bib31","doi-asserted-by":"crossref","first-page":"10548","DOI":"10.1021\/jacs.2c13647","article-title":"Liquid\u2013liquid phase separation modifies the dynamic properties of intrinsically disordered proteins","volume":"145","author":"Guseva","year":"2023","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2026.103340_bib32","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1701877114","article-title":"Direct observation of structure and dynamics during phase separation of an elastomeric protein","volume":"114","author":"Reichheld","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.sbi.2026.103340_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmr.2019.106646","article-title":"NPM1 exhibits structural and dynamic heterogeneity upon phase separation with the p14ARF tumor suppressor","volume":"310","author":"Gibbs","year":"2020","journal-title":"J Magn Reson"},{"key":"10.1016\/j.sbi.2026.103340_bib34","doi-asserted-by":"crossref","first-page":"9531","DOI":"10.1038\/s41467-024-53904-z","article-title":"p14ARF forms meso-scale assemblies upon phase separation with NPM1","volume":"15","author":"Gibbs","year":"2024","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103340_sref35","doi-asserted-by":"crossref","first-page":"3149","DOI":"10.1021\/acschemneuro.5c00181","article-title":"Exploring the structural order of condensates formed by the PRD2 domain of mouse CPEB3","volume":"16","author":"Pinhero","year":"2025","journal-title":"ACS Chem Neurosci"},{"key":"10.1016\/j.sbi.2026.103340_bib36","doi-asserted-by":"crossref","first-page":"4536","DOI":"10.1038\/s41467-019-12402-3","article-title":"Atomic-level insight into mRNA processing bodies by combining solid and solution-state NMR spectroscopy","volume":"10","author":"Damman","year":"2019","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103340_bib37","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1038\/s41467-022-28821-8","article-title":"Atomic resolution dynamics of cohesive interactions in phase-separated Nup98 FG domains","volume":"13","author":"Najbauer","year":"2022","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103340_bib38","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.ceb.2020.12.012","article-title":"The role of liquid\u2013liquid phase separation in regulating enzyme activity","volume":"69","author":"O'Flynn","year":"2021","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib39","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.sbi.2015.08.010","article-title":"Methyl groups as NMR probes for biomolecular interactions","volume":"35","author":"Wiesner","year":"2015","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib40","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.pnmrs.2019.09.004","article-title":"Methyl TROSY spectroscopy: a versatile NMR approach to study challenging biological systems","volume":"116","author":"Sch\u00fctz","year":"2020","journal-title":"Prog Nucl Magn Reson Spectrosc"},{"key":"10.1016\/j.sbi.2026.103340_bib41","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2024.102976","article-title":"Solution NMR goes big: atomic resolution studies of protein components of molecular machines and phase-separated condensates","volume":"90","author":"Sever","year":"2025","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib42","doi-asserted-by":"crossref","first-page":"7971","DOI":"10.1039\/c3cs60129c","article-title":"19F NMR: a valuable tool for studying biological events","volume":"42","author":"Chen","year":"2013","journal-title":"Chem Soc Rev"},{"key":"10.1016\/j.sbi.2026.103340_bib43","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1007\/s10858-020-00348-4","article-title":"A suite of 19F based relaxation dispersion experiments to assess biomolecular motions","volume":"74","author":"Overbeck","year":"2020","journal-title":"J Biomol NMR"},{"key":"10.1016\/j.sbi.2026.103340_bib44","doi-asserted-by":"crossref","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":"10.1016\/j.sbi.2026.103340_bib45","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2408554121","article-title":"Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates","volume":"121","author":"Ahmed","year":"2024","journal-title":"Proc Natl Acad Sci"},{"key":"10.1016\/j.sbi.2026.103340_bib46","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2508403122","article-title":"Client\u2013scaffold interactions suppress aggregation of a client protein in model condensates","volume":"122","author":"Ahmed","year":"2025","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.sbi.2026.103340_bib47","doi-asserted-by":"crossref","DOI":"10.1021\/jacs.5c10918","article-title":"Atomic resolution interactions regulating partitioning of a FUS folded RRM domain into model CAPRIN1 condensates","author":"Ahmed","year":"2025","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2026.103340_bib48","doi-asserted-by":"crossref","first-page":"7804","DOI":"10.1021\/acs.jpclett.2c01920","article-title":"Liquid\u2013liquid phase separation of an intrinsically disordered region of a germ cell-specific protein modulates the stability and conformational exchange rate of SH3 domain","volume":"13","author":"Luo","year":"2022","journal-title":"J Phys Chem Lett"},{"key":"10.1016\/j.sbi.2026.103340_bib49","article-title":"RNA modulates FUS condensate assembly, dynamics, and aggregation through diverse molecular contacts","author":"Zheng","year":"2025","journal-title":"bioRxiv"},{"key":"10.1016\/j.sbi.2026.103340_sref50","doi-asserted-by":"crossref","first-page":"19686","DOI":"10.1021\/jacs.4c06530","article-title":"Phase separation modulates the thermodynamics and kinetics of RNA hybridization","volume":"146","author":"Rangadurai","year":"2024","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2026.103340_bib51","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2026.169739","article-title":"FUS condensed phase unfolds model RNA G-quadruplex","author":"Zheng","year":"2026","journal-title":"J Mol Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib52","doi-asserted-by":"crossref","first-page":"4183","DOI":"10.1039\/D4CS01203H","article-title":"Coacervates as enzymatic microreactors","volume":"54","author":"Harris","year":"2025","journal-title":"Chem Soc Rev"},{"key":"10.1016\/j.sbi.2026.103340_bib53","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1038\/s41589-021-00774-x","article-title":"Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation","volume":"17","author":"Tibble","year":"2021","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib54","doi-asserted-by":"crossref","first-page":"3936","DOI":"10.1039\/D3SC06802A","article-title":"Deciphering the liquid\u2013liquid phase separation induced modulation in the structure, dynamics, and enzymatic activity of an ordered protein \u03b2-lactoglobulin","volume":"15","author":"Rai","year":"2024","journal-title":"Chem Sci"},{"key":"10.1016\/j.sbi.2026.103340_sref55","doi-asserted-by":"crossref","first-page":"3693","DOI":"10.1016\/j.molcel.2022.08.016","article-title":"Condensed-phase signaling can expand kinase specificity and respond to macromolecular crowding","volume":"82","author":"Sang","year":"2022","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2026.103340_bib56","doi-asserted-by":"crossref","first-page":"eabc2754","DOI":"10.1126\/science.abc2754","article-title":"Conformational states dynamically populated by a kinase determine its function","volume":"370","author":"Xie","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.sbi.2026.103340_bib57","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1038\/s41589-022-01111-6","article-title":"Observation of conformational changes that underlie the catalytic cycle of Xrn2","volume":"18","author":"Overbeck","year":"2022","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib58","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1012737","article-title":"Benchmarking residue-resolution protein coarse-grained models for simulations of biomolecular condensates","volume":"21","author":"Feito","year":"2025","journal-title":"PLoS Comput Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib59","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1038\/s41573-022-00505-4","article-title":"Modulating biomolecular condensates: a novel approach to drug discovery","volume":"21","author":"Mitrea","year":"2022","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.sbi.2026.103340_bib60","doi-asserted-by":"crossref","first-page":"1958","DOI":"10.1038\/s41594-023-01159-5","article-title":"Rational optimization of a transcription factor activation domain inhibitor","volume":"30","author":"Basu","year":"2023","journal-title":"Nat Struct Mol Biol"},{"key":"10.1016\/j.sbi.2026.103340_bib61","article-title":"How small molecules stabilize oligomers of a phase-separating disordered protein","author":"Zhu","year":"2025","journal-title":"bioRxiv"},{"key":"10.1016\/j.sbi.2026.103340_bib62","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adz7400","article-title":"Oligomerization enables the selective targeting of an intrinsically disordered region by a small molecule","volume":"12","author":"Bielskut\u0117-Garc\u00eda","year":"2026","journal-title":"Sci Adv"},{"key":"10.1016\/j.sbi.2026.103340_bib63","doi-asserted-by":"crossref","first-page":"36920","DOI":"10.1021\/jacs.5c15053","article-title":"Residue-resolved liquid-state hyperpolarized NMR of peptide condensate surfaces","volume":"147","author":"Brandis","year":"2025","journal-title":"J Am Chem Soc"}],"container-title":["Current Opinion in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X26001223?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X26001223?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T01:13:07Z","timestamp":1794273187000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959440X26001223"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":63,"alternative-id":["S0959440X26001223"],"URL":"https:\/\/doi.org\/10.1016\/j.sbi.2026.103340","relation":{},"ISSN":["0959-440X"],"issn-type":[{"value":"0959-440X","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Nuclear magnetic resonance spectroscopy as a tool to probe molecular condensates","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.sbi.2026.103340","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"103340"}}