{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T12:01:37Z","timestamp":1790769697825,"version":"4.1.0"},"reference-count":73,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:00:00Z","timestamp":1790726400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100005326","name":"Yale University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005326","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["OT2OD040572"],"award-info":[{"award-number":["OT2OD040572"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2026,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    While there is an abundance of static data for the structure of biological macromolecules, the data regarding their folding mechanisms and dynamics is scarce, posing a challenge to the training of AI models. The World Model approach, which has been very successful in robotics, can come in handy in this regard. From limited data, it can build a latent, approximated representation of the spatio\u2010temporal folding environment that can be used to train downstream AI models. Here, we developed DreamFold, a World Model\u2010based generative framework to perform biomolecular simulations. DreamFold encodes protein structures and dihedral angle moves into latent vectors using variational autoencoders. Then, it uses another neural network to rapidly predict the next latent structure after a latent move, allowing the model to develop its own understanding of protein dynamics. Finally, in a \u201challucinated\u201d latent environment, an agent learns, through evolutionary algorithms, a policy to drive folding simulations toward a target. Latent configurations can then be decoded back into atomistic structures. DreamFold can compute protein folding pathways four orders of magnitude faster than molecular dynamics (MD), up to ~30,000\u00d7. Furthermore, for the monomeric proteins tested here (up to 449\u2009aa), the computational cost scales linearly with the number of atoms (\n                    <jats:italic>N<\/jats:italic>\n                    ) as O(\n                    <jats:italic>N<\/jats:italic>\n                    ) (in comparison, MD scales as O(\n                    <jats:italic>N<\/jats:italic>\n                    log\n                    <jats:italic>N<\/jats:italic>\n                    )). We have validated our results against established MD benchmarks and other available experimental data. Finally, we show how DreamFold allows us to identify folding intermediates with cryptic binding sites that are therapeutically valuable. Overall, DreamFold facilitates the study of protein dynamics by generative AI with applications in structure\u2010based drug discovery.\n                  <\/jats:p>","DOI":"10.1002\/pro.70794","type":"journal-article","created":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T11:30:03Z","timestamp":1790767803000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["<scp>DreamFold<\/scp>\n                    : A World Model to efficiently generate protein folding pathways in the latent space"],"prefix":"10.1002","volume":"35","author":[{"given":"Alan","family":"Ianeselli","sequence":"first","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry Yale University  New Haven Connecticut USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-4873-8715","authenticated-orcid":false,"given":"Jewon","family":"Im","sequence":"additional","affiliation":[{"name":"Department of Computer Science Yale University  New Haven Connecticut USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-7657-2628","authenticated-orcid":false,"given":"Eddie","family":"Cavallin","sequence":"additional","affiliation":[{"name":"Department of Statistics and Data Science Yale University  New Haven Connecticut USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9746-3719","authenticated-orcid":false,"given":"Mark B.","family":"Gerstein","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry Yale University  New Haven Connecticut USA"},{"name":"Department of Computer Science Yale University  New Haven Connecticut USA"},{"name":"Department of Statistics and Data Science Yale University  New Haven Connecticut USA"},{"name":"Program in Computational Biology and Bioinformatics Yale University  New Haven Connecticut USA"},{"name":"Department of Biomedical Informatics &amp; Data Science Yale University  New Haven Connecticut USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,30]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"crossref","first-page":"17442","DOI":"10.1073\/pnas.1209000109","article-title":"De novo prediction of protein folding pathways and structure using the principle of sequential stabilization","volume":"109","author":"Adhikari AN","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"e_1_2_9_3_1","doi-asserted-by":"crossref","first-page":"3031","DOI":"10.1021\/acs.jctc.7b00125","article-title":"The Rosetta all\u2010atom energy function for macromolecular modeling and design","volume":"13","author":"Alford RF","year":"2017","journal-title":"J Chem Theory Comput"},{"key":"e_1_2_9_4_1","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1007\/s10867-017-9470-7","article-title":"Temperature evolution of Trp\u2010cage folding pathways: an analysis by dividing the probability flux field into stream tubes","volume":"43","author":"Andryushchenko VA","year":"2017","journal-title":"J Biol Phys"},{"key":"e_1_2_9_5_1","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1016\/j.str.2016.05.022","article-title":"Domain\u2010swapped dimers of intracellular lipid\u2010binding proteins: evidence for ordered folding intermediates","volume":"24","author":"Assar Z","year":"2016","journal-title":"Structure"},{"key":"e_1_2_9_6_1","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1073\/pnas.1111796109","article-title":"Dominant folding pathways of a WW domain","volume":"109","author":"Beccara SA","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1002\/PROT.26479"},{"key":"e_1_2_9_8_1","doi-asserted-by":"crossref","first-page":"6011","DOI":"10.1021\/bi501021r","article-title":"Folding dynamics and pathways of the Trp\u2010cage miniproteins","volume":"53","author":"Byrne A","year":"2014","journal-title":"Biochemistry"},{"key":"e_1_2_9_9_1","doi-asserted-by":"crossref","DOI":"10.1063\/1.3523345","article-title":"Hierarchy of folding and unfolding events of protein G, CI2, and ACBP from explicit\u2010solvent simulations","volume":"134","author":"Camilloni C","year":"2011","journal-title":"J Chem Phys"},{"key":"e_1_2_9_10_1","doi-asserted-by":"crossref","first-page":"1424","DOI":"10.1110\/ps.035105.108","article-title":"Early events in protein folding: is there something more than hydrophobic burst?","volume":"17","author":"Camilloni C","year":"2008","journal-title":"Protein Sci"},{"key":"e_1_2_9_11_1","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1093\/bioinformatics\/btq007","article-title":"PyRosetta: a script\u2010based interface for implementing molecular modeling algorithms using Rosetta","volume":"26","author":"Chaudhury S","year":"2010","journal-title":"Bioinformatics"},{"key":"e_1_2_9_12_1","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all\u2010atom structure validation for macromolecular crystallography","volume":"66","author":"Chen VB","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_9_13_1","doi-asserted-by":"crossref","first-page":"10884","DOI":"10.1002\/anie.201104085","article-title":"Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp\u2010cage","volume":"50","author":"Culik RM","year":"2011","journal-title":"Angew Chem Int Ed Engl"},{"key":"e_1_2_9_14_1","first-page":"9156","volume-title":"Thirty\u2010seventh Conference on Neural Information Processing Systems","author":"Du Y","year":"2023"},{"key":"e_1_2_9_15_1","doi-asserted-by":"crossref","first-page":"L53","DOI":"10.1016\/j.bpj.2009.01.024","article-title":"The Fip35 WW domain folds with structural and mechanistic heterogeneity in molecular dynamics simulations","volume":"96","author":"Ensign DL","year":"2009","journal-title":"Biophys J"},{"key":"e_1_2_9_16_1","first-page":"1","volume-title":"IEEE Trans Intell Veh","author":"Guan Y","year":"2024"},{"key":"e_1_2_9_17_1","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/s42003-022-03562-y","article-title":"Artificial intelligence guided conformational mining of intrinsically disordered proteins","volume":"5","author":"Gupta A","year":"2022","journal-title":"Commun Biol"},{"key":"e_1_2_9_18_1","first-page":"2450","article-title":"Recurrent world models facilitate policy evolution","volume":"31","author":"Ha D","year":"2018","journal-title":"Adv Neural Inf Process Syst"},{"key":"e_1_2_9_19_1","volume-title":"International Conference on Learning Representations","author":"Hafner D","year":"2021"},{"key":"e_1_2_9_20_1","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/3-540-32494-1_4","volume-title":"Towards a new evolutionary computation: advances in the estimation of distribution algorithms","author":"Hansen N","year":"2006"},{"key":"e_1_2_9_21_1","doi-asserted-by":"crossref","unstructured":"IaneselliA HowardJ GersteinMB.A discard\u2010and\u2010restart MD algorithm for the sampling of realistic protein transition states and enhance structure\u2010based drug discovery. bioRxiv 2024.06.14.598892.2024https:\/\/doi.org\/10.1101\/2024.06.14.598892","DOI":"10.1101\/2024.06.14.598892"},{"key":"e_1_2_9_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpj.2025.03.024"},{"key":"e_1_2_9_23_1","doi-asserted-by":"crossref","first-page":"3674","DOI":"10.1021\/jacs.7b12399","article-title":"Atomic detail of protein folding revealed by an ab initio reappraisal of circular dichroism","volume":"140","author":"Ianeselli A","year":"2018","journal-title":"J Am Chem Soc"},{"key":"e_1_2_9_24_1","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1038\/s42004-025-01737-2","article-title":"Deep generative modeling of temperature\u2010dependent structural ensembles of proteins","volume":"8","author":"Janson G","year":"2025","journal-title":"Commun Chem"},{"key":"e_1_2_9_25_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1145\/3571730","article-title":"Survey of hallucination in natural language generation","volume":"55","author":"Ji Z","year":"2023","journal-title":"ACM Comput Surv"},{"key":"e_1_2_9_26_1","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1529\/biophysj.107.116095","article-title":"Folding pathway of the B1 domain of protein G explored by multiscale modeling","volume":"94","author":"Kmiecik S","year":"2008","journal-title":"Biophys J"},{"key":"e_1_2_9_27_1","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1002\/prot.340180405","article-title":"Monte Carlo simulations of protein folding. I. Lattice model and interaction scheme","volume":"18","author":"Kolinski A","year":"1994","journal-title":"Proteins"},{"key":"e_1_2_9_28_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13321-018-0285-8","article-title":"P2Rank: machine learning based tool for rapid and accurate prediction of ligand binding sites from protein structure","volume":"10","author":"Kriv\u00e1k R","year":"2018","journal-title":"J Cheminform"},{"key":"e_1_2_9_29_1","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1214\/aoms\/1177729694","article-title":"On information and sufficiency","volume":"22","author":"Kullback S","year":"1951","journal-title":"Ann Math Stat"},{"key":"e_1_2_9_30_1","doi-asserted-by":"crossref","DOI":"10.1088\/0034-4885\/71\/12\/126601","article-title":"Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science","volume":"71","author":"Laio A","year":"2008","journal-title":"Rep Prog Phys"},{"key":"e_1_2_9_31_1","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1016\/j.bpj.2014.06.037","article-title":"Complex pathways in folding of protein G explored by simulation and experiment","volume":"107","author":"Lapidus LJ","year":"2014","journal-title":"Biophys J"},{"key":"e_1_2_9_32_1","doi-asserted-by":"crossref","DOI":"10.1126\/science.adv9817","article-title":"Scalable emulation of protein equilibrium ensembles with generative deep learning","volume":"389","author":"Lewis S","year":"2025","journal-title":"Science"},{"key":"e_1_2_9_33_1","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1126\/science.1208351","article-title":"How fast\u2010folding proteins fold","volume":"334","author":"Lindorff\u2010Larsen K","year":"2011","journal-title":"Science"},{"key":"e_1_2_9_34_1","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1016\/j.jmb.2010.01.071","article-title":"A survey of lambda repressor fragments from two\u2010state to downhill folding","volume":"397","author":"Liu F","year":"2010","journal-title":"J Mol Biol"},{"key":"e_1_2_9_35_1","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1021\/jz300017c","article-title":"Structural characterization of \u03bb\u2010repressor folding from all\u2010atom molecular dynamics simulations","volume":"3","author":"Liu Y","year":"2012","journal-title":"J Phys Chem Lett"},{"key":"e_1_2_9_36_1","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1006\/jmbi.1999.2544","article-title":"The structure and dynamics of rat apo\u2010cellular retinol\u2010binding protein II in solution: comparison with the X\u2010ray structure","volume":"286","author":"Lu J","year":"1999","journal-title":"J Mol Biol"},{"key":"e_1_2_9_37_1","doi-asserted-by":"crossref","first-page":"2689","DOI":"10.1021\/acs.jctc.3c01057","article-title":"Protein ensemble generation through variational autoencoder latent space sampling","volume":"20","author":"Mansoor S","year":"2024","journal-title":"J Chem Theory Comput"},{"key":"e_1_2_9_38_1","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1038\/77971","article-title":"Critical role of beta\u2010hairpin formation in protein G folding","volume":"7","author":"McCallister EL","year":"2000","journal-title":"Nat Struct Biol"},{"key":"e_1_2_9_39_1","doi-asserted-by":"crossref","first-page":"11490","DOI":"10.1021\/jp404714c","article-title":"Folding dynamics of the trp\u2010cage miniprotein: evidence for a native\u2010like intermediate from combined time\u2010resolved vibrational spectroscopy and molecular dynamics simulations","volume":"117","author":"Meuzelaar H","year":"2013","journal-title":"J Phys Chem B"},{"key":"e_1_2_9_40_1","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/nature05728","article-title":"A pre\u2010existing hydrophobic collapse in the unfolded state of an ultrafast folding protein","volume":"447","author":"Mok KH","year":"2007","journal-title":"Nature"},{"key":"e_1_2_9_41_1","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/j.bpj.2011.09.013","article-title":"GB1 is not a two\u2010state folder: identification and characterization of an on\u2010pathway intermediate","volume":"101","author":"Morrone A","year":"2011","journal-title":"Biophys J"},{"key":"e_1_2_9_42_1","doi-asserted-by":"crossref","DOI":"10.1142\/S0219633614500266","article-title":"Folding simulation of Trp\u2010cage utilizing a new AMBER compatible force field with coupled main chain torsions","volume":"13","author":"Mou L","year":"2014","journal-title":"J Theor Comput Chem"},{"key":"e_1_2_9_43_1","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.sbi.2008.01.008","article-title":"Transition networks for modeling the kinetics of conformational change in macromolecules","volume":"18","author":"No\u00e9 F","year":"2008","journal-title":"Curr Opin Struct Biol"},{"key":"e_1_2_9_44_1","doi-asserted-by":"crossref","first-page":"152724","DOI":"10.1063\/1.5006039","article-title":"All\u2010atom calculation of protein free\u2010energy profiles","volume":"147","author":"Orioli S","year":"2017","journal-title":"J Chem Phys"},{"key":"e_1_2_9_45_1","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips JC","year":"2005","journal-title":"J Comput Chem"},{"key":"e_1_2_9_46_1","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1529\/biophysj.104.042861","article-title":"Variations in the fast folding rates of the lambda\u2010repressor: a hybrid molecular dynamics study","volume":"87","author":"Pogorelov TV","year":"2004","journal-title":"Biophys J"},{"key":"e_1_2_9_47_1","doi-asserted-by":"crossref","first-page":"27718","DOI":"10.1074\/jbc.M111.234393","article-title":"A survey of antiprion compounds reveals the prevalence of non\u2010PrP molecular targets","volume":"286","author":"Poncet\u2010Montange G","year":"2011","journal-title":"J Biol Chem"},{"key":"e_1_2_9_48_1","doi-asserted-by":"crossref","first-page":"2090","DOI":"10.1021\/jp110175x","article-title":"Reducing lambda repressor to the core","volume":"115","author":"Prigozhin MB","year":"2011","journal-title":"J Phys Chem B"},{"key":"e_1_2_9_49_1","doi-asserted-by":"crossref","first-page":"1268","DOI":"10.1016\/j.bbapap.2014.04.011","article-title":"The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins","volume":"1844","author":"Ragona L","year":"2014","journal-title":"Biochim Biophys Acta Proteins Proteom"},{"key":"e_1_2_9_50_1","doi-asserted-by":"crossref","first-page":"2147","DOI":"10.1016\/j.str.2024.09.001","article-title":"Assessing AF2's ability to predict structural ensembles of proteins","volume":"32","author":"Riccabona JR","year":"2024","journal-title":"Structure"},{"key":"e_1_2_9_51_1","volume-title":"The Thirty\u2010eighth Annual Conference on Neural Information Processing Systems","author":"Saanum T","year":"2024"},{"key":"e_1_2_9_52_1","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1038\/s41586-020-03051-4","article-title":"Mastering Atari, go, chess and shogi by planning with a learned model","volume":"588","author":"Schrittwieser J","year":"2020","journal-title":"Nature"},{"key":"e_1_2_9_53_1","doi-asserted-by":"crossref","DOI":"10.1063\/1.4895044","article-title":"Perspective: Markov models for long\u2010timescale biomolecular dynamics","volume":"141","author":"Schwantes CR","year":"2014","journal-title":"J Chem Phys"},{"key":"e_1_2_9_54_1","unstructured":"SchwingG PaleseLL Fern\u00e1ndezA SchwiebertL GattiDL.Molecular dynamics without molecules: searching the conformational space of proteins with generative neural networks. arXiv2022 https:\/\/doi.org\/10.48550\/arXiv.2206.04683."},{"key":"e_1_2_9_55_1","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1126\/science.1187409","article-title":"Atomic\u2010level characterization of the structural dynamics of proteins","volume":"330","author":"Shaw DE","year":"2010","journal-title":"Science"},{"key":"e_1_2_9_56_1","doi-asserted-by":"crossref","first-page":"8528","DOI":"10.1074\/jbc.M116.714535","article-title":"Ligand binding induces conformational changes in human cellular retinol\u2010binding protein 1 (CRBP1) revealed by atomic resolution crystal structures","volume":"291","author":"Silvaroli JA","year":"2016","journal-title":"J Biol Chem"},{"key":"e_1_2_9_57_1","doi-asserted-by":"crossref","first-page":"15975","DOI":"10.1073\/pnas.1404213111","article-title":"Benchmarking all\u2010atom simulations using hydrogen exchange","volume":"111","author":"Skinner JJ","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"e_1_2_9_58_1","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1016\/j.str.2020.08.005","article-title":"A global Ramachandran score identifies protein structures with unlikely stereochemistry","volume":"28","author":"Sobolev OV","year":"2020","journal-title":"Structure"},{"key":"e_1_2_9_59_1","doi-asserted-by":"crossref","first-page":"17377","DOI":"10.1073\/pnas.0407683101","article-title":"Differences in the folding transition state of ubiquitin indicated by phi and psi analyses","volume":"101","author":"Sosnick TR","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"e_1_2_9_60_1","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1038\/s41592-021-01098-3","article-title":"Martini 3: a general purpose force field for coarse\u2010grained molecular dynamics","volume":"18","author":"Souza PCT","year":"2021","journal-title":"Nat Methods"},{"key":"e_1_2_9_61_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s42003-020-01585-x","article-title":"Pharmacological inactivation of the prion protein by targeting a folding intermediate","volume":"4","author":"Spagnolli G","year":"2021","journal-title":"Commun Biol"},{"key":"e_1_2_9_62_1","doi-asserted-by":"crossref","first-page":"2948","DOI":"10.1021\/acs.jctc.0c00933","article-title":"Long\u2010time\u2010scale predictions from short\u2010trajectory data: a benchmark analysis of the Trp\u2010cage miniprotein","volume":"17","author":"Strahan J","year":"2021","journal-title":"J Chem Theory Comput"},{"key":"e_1_2_9_63_1","doi-asserted-by":"crossref","first-page":"248","DOI":"10.2142\/biophysico.16.0_248","article-title":"G\u014d model revisited","volume":"16","author":"Takada S","year":"2019","journal-title":"Biophys Physicobiol"},{"key":"e_1_2_9_64_1","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.781635","article-title":"Explore protein conformational space with variational autoencoder","volume":"8","author":"Tian H","year":"2021","journal-title":"Front Mol Biosci"},{"key":"e_1_2_9_65_1","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1021\/acs.jcim.2c01213","article-title":"LAST: latent space\u2010assisted adaptive sampling for protein trajectories","volume":"63","author":"Tian H","year":"2023","journal-title":"J Chem Inf Model"},{"key":"e_1_2_9_66_1","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/j.jmb.2006.08.059","article-title":"The structure of Apo\u2010wild\u2010type cellular retinoic acid binding protein II at 1.4\u2009\u00c5 and its relationship to ligand binding and nuclear translocation","volume":"363","author":"Vaezeslami S","year":"2006","journal-title":"J Mol Biol"},{"key":"e_1_2_9_67_1","doi-asserted-by":"crossref","first-page":"2083","DOI":"10.1016\/j.bpj.2018.03.027","article-title":"All\u2010atom simulations reveal how single\u2010point mutations promote serpin misfolding","volume":"114","author":"Wang F","year":"2018","journal-title":"Biophys J"},{"key":"e_1_2_9_68_1","first-page":"55","volume-title":"Computer vision \u2013 ECCV 2024","author":"Wang X","year":"2025"},{"key":"e_1_2_9_69_1","volume-title":"6th Annual Conference on Robot Learning","author":"Wu P","year":"2022"},{"key":"e_1_2_9_70_1","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1016\/j.bpj.2020.10.003","article-title":"Residual structure of unfolded ubiquitin as revealed by hydrogen\/deuterium\u2010exchange 2D NMR","volume":"119","author":"Yagi\u2010Utsumi M","year":"2020","journal-title":"Biophys J"},{"key":"e_1_2_9_71_1","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1529\/biophysj.103.039040","article-title":"Folding \u03bb\u2010repressor at its speed limit","volume":"87","author":"Yang WY","year":"2004","journal-title":"Biophys J"},{"key":"e_1_2_9_72_1","doi-asserted-by":"crossref","first-page":"13280","DOI":"10.1073\/pnas.2233312100","article-title":"Trp\u2010cage: folding free energy landscape in explicit water","volume":"100","author":"Zhou R","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"e_1_2_9_73_1","doi-asserted-by":"crossref","first-page":"bbad429","DOI":"10.1093\/bib\/bbad429","article-title":"Phanto\u2010IDP: compact model for precise intrinsically disordered protein backbone generation and enhanced sampling","volume":"25","author":"Zhu J","year":"2023","journal-title":"Brief Bioinform"},{"key":"e_1_2_9_74_1","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1073\/pnas.89.1.20","article-title":"Levinthal's paradox","volume":"89","author":"Zwanzig R","year":"1992","journal-title":"Proc Natl Acad Sci U S A"}],"container-title":["Protein Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/pro.70794","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/full-xml\/10.1002\/pro.70794","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/pro.70794","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T11:30:16Z","timestamp":1790767816000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/pro.70794"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,30]]},"references-count":73,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2026,11]]}},"alternative-id":["10.1002\/pro.70794"],"URL":"https:\/\/doi.org\/10.1002\/pro.70794","archive":["Portico"],"relation":{},"ISSN":["0961-8368","1469-896X"],"issn-type":[{"value":"0961-8368","type":"print"},{"value":"1469-896X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,30]]},"assertion":[{"value":"2026-04-30","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-08-31","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-09-30","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"e70794"}}