{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T06:46:00Z","timestamp":1789713960958,"version":"4.0.1"},"reference-count":90,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2019,8,13]],"date-time":"2019-08-13T00:00:00Z","timestamp":1565654400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006228","name":"Oak Ridge National Laboratory","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006228","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Biosci."],"DOI":"10.3389\/fmolb.2019.00064","type":"journal-article","created":{"date-parts":[[2019,8,13]],"date-time":"2019-08-13T01:18:43Z","timestamp":1565659123000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":32,"title":["Using Small-Angle Scattering Data and Parametric Machine Learning to Optimize Force Field Parameters for Intrinsically Disordered Proteins"],"prefix":"10.3389","volume":"6","author":[{"given":"Omar","family":"Demerdash","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Utsab R.","family":"Shrestha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Loukas","family":"Petridis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremy C.","family":"Smith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie C.","family":"Mitchell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arvind","family":"Ramanathan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2019,8,13]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"Gromacs: high performance molecular simulations through multi-level parallelism from laptops to supercomputers","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"B2","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1126\/science.181.4096.223","article-title":"Principles that govern the folding of protein chains","volume":"181","author":"Anfinsen","year":"1973","journal-title":"Science"},{"key":"B3","doi-asserted-by":"publisher","first-page":"9614","DOI":"10.1073\/pnas.1512799112","article-title":"Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding","volume":"112","author":"Arai","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B4","doi-asserted-by":"publisher","first-page":"630","DOI":"10.1016\/j.str.2017.02.011","article-title":"The unique domain forms a fuzzy intramolecular complex in src family kinases","volume":"25","author":"Arbes\u00fc","year":"2017","journal-title":"Structure"},{"key":"B5","doi-asserted-by":"publisher","first-page":"3684","DOI":"10.1063\/1.448118","article-title":"Molecular-dynamics with coupling to an external bath","volume":"81","author":"Berendsen","year":"1984","journal-title":"J. Chem. Phys."},{"key":"B6","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":"B7","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1039\/c1mb05275f","article-title":"Structural analysis of intrinsically disordered proteins by small-angle x-ray scattering","volume":"8","author":"Bernad\u00f3","year":"2012","journal-title":"Mol. Biosyst."},{"key":"B8","doi-asserted-by":"publisher","first-page":"14916","DOI":"10.1021\/jp108618d","article-title":"Protein simulations with an optimized water model: cooperative helix formation and temperature-induced unfolded state collapse","volume":"114","author":"Best","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"B9","doi-asserted-by":"publisher","first-page":"eaar7101","DOI":"10.1126\/science.aar7101","article-title":"Comment on \u201cinnovative scattering analysis shows that hydrophobic disordered proteins are expanded in water.\u201d","volume":"361","author":"Best","year":"2018","journal-title":"Science"},{"key":"B10","doi-asserted-by":"publisher","first-page":"5113","DOI":"10.1021\/ct500569b","article-title":"Balanced protein-water interactions improve properties of disordered proteins and non-specific protein association","volume":"10","author":"Best","year":"2014","journal-title":"J. Chem. Theor. Comput."},{"key":"B11","doi-asserted-by":"publisher","first-page":"E146","DOI":"10.3390\/biom9040146","article-title":"Recent advances in computational protocols addressing intrinsically disordered proteins","volume":"9","author":"Bhattacharya","year":"2019","journal-title":"Biomolecules"},{"key":"B12","first-page":"108","article-title":"API design for machine learning software: experiences from the scikit-learn project","volume-title":"ECML PKDD Workshop: Languages for Data Mining and Machine Learning","author":"Buitinck","year":"2013"},{"key":"B13","doi-asserted-by":"publisher","first-page":"7875","DOI":"10.1038\/ncomms8875","article-title":"Intrinsically disordered proteins drive membrane curvature","volume":"6","author":"Busch","year":"2015","journal-title":"Nat. Commun."},{"key":"B14","doi-asserted-by":"publisher","first-page":"1463","DOI":"10.1093\/bioinformatics\/bts172","article-title":"Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables","volume":"28","author":"Charavay","year":"2012","journal-title":"Bioinformatics"},{"key":"B15","doi-asserted-by":"publisher","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh ewald\u2013an n.log(n) method for ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"B16","doi-asserted-by":"publisher","first-page":"13392","DOI":"10.1073\/pnas.1304749110","article-title":"Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues","volume":"110","author":"Das","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B17","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1145\/355958.355966","article-title":"An adaptive nonlinear least-squares algorithm","volume":"7","author":"Dennis John","year":"1981","journal-title":"ACM Trans. Math. Softw."},{"key":"B18","doi-asserted-by":"publisher","first-page":"560","DOI":"10.1107\/S2059798318006496","article-title":"Approaches to altering particle distributions in cryo-electron microscopy sample preparation","volume":"74","author":"Drulyte","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"B19","doi-asserted-by":"publisher","first-page":"1212","DOI":"10.1107\/S1600576717007786","article-title":"Atsas 2.8: a comprehensive data analysis suite for small-angle scattering from macromolecular solutions","volume":"50","author":"Franke","year":"2017","journal-title":"J. Appl. Crystallogr."},{"key":"B20","doi-asserted-by":"publisher","first-page":"E6342","DOI":"10.1073\/pnas.1704692114","article-title":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in saxs vs. fret measurements","volume":"114","author":"Fuertes","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B21","doi-asserted-by":"publisher","first-page":"16621","DOI":"10.1021\/ja054342m","article-title":"Refinement of multidomain protein structures by combination of solution small-angle x-ray scattering and nmr data","volume":"127","author":"Grishaev","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"B22","doi-asserted-by":"publisher","first-page":"6561","DOI":"10.1021\/cr400514h","article-title":"Introducing protein intrinsic disorder","volume":"114","author":"Habchi","year":"2014","journal-title":"Chem. Rev."},{"key":"B23","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1007\/s10858-011-9478-4","article-title":"Shiftx2: significantly improved protein chemical shift prediction","volume":"50","author":"Han","year":"2011","journal-title":"J. Biomol. NMR"},{"key":"B24","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1021\/ct700200b","article-title":"P-lincs: a parallel linear constraint solver for molecular simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J. Chem. Theor. Comput."},{"key":"B25","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"Lincs: a linear constraint solver for molecular simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J. Comput. Chem."},{"key":"B26","doi-asserted-by":"publisher","first-page":"16155","DOI":"10.1073\/pnas.1207719109","article-title":"Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy","volume":"109","author":"Hofmann","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B27","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1016\/j.bpj.2016.11.3200","article-title":"Cider: resources to analyze sequence-ensemble relationships of intrinsically disordered proteins","volume":"112","author":"Holehouse","year":"2017","journal-title":"Biophys. J."},{"key":"B28","doi-asserted-by":"publisher","first-page":"9665","DOI":"10.1063\/1.1683075","article-title":"Development of an improved four-site water model for biomolecular simulations: Tip4p-ew","volume":"120","author":"Horn","year":"2004","journal-title":"J. Chem. Phys."},{"key":"B29","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.sbi.2017.10.008","article-title":"Force field development and simulations of intrinsically disordered proteins","volume":"48","author":"Huang","year":"2018","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B30","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1038\/Nmeth.4067","article-title":"Charmm36m: an improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nat. Methods"},{"key":"B31","doi-asserted-by":"publisher","first-page":"6632","DOI":"10.1021\/cr400688u","article-title":"Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using nmr spectroscopy","volume":"114","author":"Jensen","year":"2014","journal-title":"Chem. Rev."},{"key":"B32","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1021\/ar020082r","article-title":"Molecular dynamics simulations of biomolecules","volume":"35","author":"Karplus","year":"2002","journal-title":"Acc. Chem. Res."},{"key":"B33","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":"B34","doi-asserted-by":"publisher","first-page":"2570","DOI":"10.1016\/j.febslet.2015.08.027","article-title":"A practical guide to small angle x-ray scattering (saxs) of flexible and intrinsically disordered proteins","volume":"589","author":"Kikhney","year":"2015","journal-title":"FEBS Lett."},{"key":"B35","doi-asserted-by":"publisher","first-page":"384","DOI":"10.1038\/nrm3810","article-title":"The amyloid state and its association with protein misfolding diseases","volume":"15","author":"Knowles","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B36","doi-asserted-by":"publisher","first-page":"6999","DOI":"10.1038\/s41598-017-07156-1","article-title":"Predictions of backbone dynamics in intrinsically disordered proteins using de novo fragment-based protein structure predictions","volume":"7","author":"Kosciolek","year":"2017","journal-title":"Sci. Rep."},{"key":"B37","doi-asserted-by":"publisher","first-page":"909","DOI":"10.1002\/pro.2674","article-title":"How do disordered regions achieve comparable functions to structured domains?","volume":"24","author":"Latysheva","year":"2015","journal-title":"Protein Sci."},{"key":"B38","doi-asserted-by":"publisher","first-page":"9423","DOI":"10.1021\/jp510896n","article-title":"Revised parameters for the amoeba polarizable atomic multipole water model","volume":"119","author":"Laury","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"B39","doi-asserted-by":"publisher","first-page":"431","DOI":"10.5483\/BMBRep.2016.49.8.021","article-title":"Structural investigation on the intrinsically disordered n-terminal region of hpv16 e7 protein","volume":"49","author":"Lee","year":"2016","journal-title":"BMB Rep."},{"key":"B40","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1002\/jcc.23957","article-title":"Multiscale enhanced sampling of intrinsically disordered protein conformations","volume":"37","author":"Lee","year":"2016","journal-title":"J. Comput. Chem."},{"key":"B41","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1090\/qam\/10666","article-title":"A method for the solution of certain non-linear problems in least squares","volume":"2","author":"Levenberg","year":"1944","journal-title":"Q. Appl. Math."},{"key":"B42","doi-asserted-by":"publisher","first-page":"2758","DOI":"10.1073\/pnas.1418155112","article-title":"Regulation and aggregation of intrinsically disordered peptides","volume":"112","author":"Levine","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B43","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1007\/978-1-4939-1465-4_3","article-title":"Current status of protein force fields for molecular dynamics simulations","volume":"1215","author":"Lopes","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"B44","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1137\/0111030","article-title":"An algortithm for least-squares estimation of nonlinear parameters","volume":"11","author":"Marquardt","year":"1963","journal-title":"J. Soc. Indus. Appl. Math."},{"key":"B45","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1016\/j.jmb.2009.06.001","article-title":"Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints","volume":"391","author":"Marsh","year":"2009","journal-title":"J. Mol. Biol."},{"key":"B46","doi-asserted-by":"publisher","first-page":"1494","DOI":"10.1016\/j.jmb.2007.01.038","article-title":"Improved structural characterizations of the drkn sh3 domain unfolded state suggest a compact ensemble with native-like and non-native structure","volume":"367","author":"Marsh","year":"2007","journal-title":"J. Mol. Biol."},{"key":"B47","doi-asserted-by":"publisher","first-page":"52","DOI":"10.3389\/fmolb.2016.00052","article-title":"Binding mechanisms of intrinsically disordered proteins: theory, simulation, and experiment","volume":"3","author":"Mollica","year":"2016","journal-title":"Front. Mol. Biosci."},{"key":"B48","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1137\/0904038","article-title":"Computing a trust region step","volume":"4","author":"More","year":"1983","journal-title":"SIAM J. Sci. Stat. Comput."},{"key":"B49","doi-asserted-by":"publisher","first-page":"1220","DOI":"10.1021\/ct2000183","article-title":"Optimizing protein-solvent force fields to reproduce intrinsic conformational preferences of model peptides","volume":"7","author":"Nerenberg","year":"2011","journal-title":"J. Chem. Theor. Comput."},{"key":"B50","doi-asserted-by":"publisher","first-page":"20740","DOI":"10.1073\/pnas.0900622106","article-title":"Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins","volume":"106","author":"Nettels","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B51","doi-asserted-by":"publisher","first-page":"566","DOI":"10.1002\/prot.10532","article-title":"Predicting intrinsic disorder from amino acid sequence","volume":"53","author":"Obradovic","year":"2003","journal-title":"Proteins"},{"key":"B52","doi-asserted-by":"publisher","first-page":"7182","DOI":"10.1063\/1.328693","article-title":"Polymorphic transitions in single crystals: a new molecular dynamics method","volume":"52","author":"Parrinello","year":"1981","journal-title":"J. Appl. Phys."},{"key":"B53","unstructured":"Scikit-learn: machine learning in Python28252830\n            PedregosaF.\n            VaroquauxG.\n            GramfortA.\n            MichelV.\n            ThirionB.\n            GriselO.\n          J. Mach. Learn. Res.122011"},{"key":"B54","doi-asserted-by":"publisher","first-page":"174","DOI":"10.4149\/gpb_2009_02_174","article-title":"Structure and flexibility within proteins as identified through small angle x-ray scattering","volume":"28","author":"Pelikan","year":"2009","journal-title":"Gen. Physiol. Biophys."},{"key":"B55","doi-asserted-by":"publisher","first-page":"136","DOI":"10.1016\/j.jmb.2009.06.018","article-title":"Structural characterization of the natively unfolded n-terminal domain of human c-src kinase: insights into the role of phosphorylation of the unique domain","volume":"391","author":"P\u00e9rez","year":"2009","journal-title":"J. Mol. Biol."},{"key":"B56","doi-asserted-by":"publisher","first-page":"1295","DOI":"10.1038\/srep01295","article-title":"Lipid binding by the unique and sh3 domains of c-src suggests a new regulatory mechanism","volume":"3","author":"P\u00e9rez","year":"2013","journal-title":"Sci. Rep."},{"key":"B57","doi-asserted-by":"publisher","first-page":"5113","DOI":"10.1021\/jp508971m","article-title":"Water dispersion interactions strongly influence simulated structural properties of disordered protein states","volume":"119","author":"Piana","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"B58","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1016\/j.sbi.2013.12.006","article-title":"Assessing the accuracy of physical models used in protein-folding simulations: quantitative evidence from long molecular dynamics simulations","volume":"24","author":"Piana","year":"2014","journal-title":"Curr. Opin. Struct. Biol."},{"key":"B59","doi-asserted-by":"publisher","first-page":"5513","DOI":"10.1021\/acs.jctc.5b00736","article-title":"Structural ensembles of intrinsically disordered proteins depend strongly on force field: a comparison to experiment","volume":"11","author":"Rauscher","year":"2015","journal-title":"J. Chem. Theor. Comput."},{"key":"B60","doi-asserted-by":"publisher","first-page":"55","DOI":"10.2174\/138920312799277901","article-title":"How random are intrinsically disordered proteins? a small angle scattering perspective","volume":"13","author":"Receveur-Br\u00e9chot","year":"2012","journal-title":"Curr. Protein Pept. Sci."},{"key":"B61","doi-asserted-by":"publisher","first-page":"eaar7949","DOI":"10.1126\/science.aar7949","article-title":"Response to comment on \u201cinnovative scattering analysis shows that hydrophobic disordered proteins are expanded in water\u201d?","volume":"361","author":"Riback","year":"2018","journal-title":"Science"},{"key":"B62","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1126\/science.aan5774","article-title":"Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water","volume":"358","author":"Riback","year":"2017","journal-title":"Science"},{"key":"B63","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":"B64","doi-asserted-by":"publisher","first-page":"6365","DOI":"10.1021\/ja300265w","article-title":"Interpreting protein structural dynamics from nmr chemical shifts","volume":"134","author":"Robustelli","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"B65","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1016\/j.str.2010.10.006","article-title":"Saxs ensemble refinement of escrt-iii chmp3 conformational transitions","volume":"19","author":"Rozycki","year":"2011","journal-title":"Structure"},{"key":"B66","doi-asserted-by":"publisher","first-page":"13026","DOI":"10.1021\/ja105485b","article-title":"Solution structure of the 128 kda enzyme i dimer from escherichia coli and its 146 kda complex with hpr using residual dipolar couplings and small- and wide-angle x-ray scattering","volume":"132","author":"Schwieters","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"B67","doi-asserted-by":"publisher","first-page":"134508","DOI":"10.1063\/1.1877132","article-title":"Solvation free energies of amino acid side chain analogs for common molecular mechanics water models","volume":"122","author":"Shirts","year":"2005","journal-title":"J. Chem. Phys."},{"key":"B68","doi-asserted-by":"publisher","first-page":"5740","DOI":"10.1063\/1.1587119","article-title":"Extremely precise free energy calculations of amino acid side chain analogs: comparison of common molecular mechanics force fields for proteins","volume":"119","author":"Shirts","year":"2003","journal-title":"J. Chem. Phys."},{"key":"B69","doi-asserted-by":"publisher","first-page":"15975","DOI":"10.1073\/pnas.1404213111","article-title":"Benchmarking all-atom simulations using hydrogen exchange","volume":"111","author":"Skinner","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B70","doi-asserted-by":"publisher","first-page":"1166","DOI":"10.1021\/acs.jcim.7b00135","article-title":"The idp-specific force field ff14idpsff improves the conformer sampling of intrinsically disordered proteins","volume":"57","author":"Song","year":"2017","journal-title":"J. Chem. Inform. Model."},{"key":"B71","doi-asserted-by":"publisher","first-page":"1589","DOI":"10.1016\/j.jmb.2016.03.007","article-title":"A unique hetero-hexadecameric architecture displayed by the escherichia coli o157 paaa2-pare2 antitoxin-toxin complex","volume":"428","author":"Sterckx","year":"2016","journal-title":"J. Mol. Biol."},{"key":"B72","doi-asserted-by":"publisher","first-page":"854","DOI":"10.1016\/j.str.2014.03.012","article-title":"Small-angle x-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin paaa2","volume":"22","author":"Sterckx","year":"2014","journal-title":"Structure"},{"key":"B73","doi-asserted-by":"publisher","first-page":"768","DOI":"10.1107\/S0021889895007047","article-title":"Crysol\u2013a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates","volume":"28","author":"Svergun","year":"1995","journal-title":"J. Appl. Crystallogr."},{"key":"B74","unstructured":"Kinases of the src family: structure and functions4958\n            TatosyanA. G.\n            MizeninaO. A.\n          10702640Biochemistry652000"},{"key":"B75","doi-asserted-by":"publisher","first-page":"E386","DOI":"10.1073\/pnas.1424461112","article-title":"Kinetics of protein\u2013ligand unbinding: predicting pathways, rates, and rate-limiting steps","volume":"112","author":"Tiwary","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B76","doi-asserted-by":"publisher","first-page":"1090","DOI":"10.1016\/j.biocel.2011.04.001","article-title":"Intrinsically disordered proteins from a to z","volume":"43","author":"Uversky","year":"2011","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"B77","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1146\/annurev.biophys.37.032807.125924","article-title":"Intrinsically disordered proteins in human diseases: introducing the d2 concept","volume":"37","author":"Uversky","year":"2008","journal-title":"Annu. Rev. Biophys."},{"key":"B78","doi-asserted-by":"publisher","first-page":"1829","DOI":"10.1021\/pr0602388","article-title":"Protein intrinsic disorder and human papillomaviruses: increased amount of disorder in e6 and e7 oncoproteins from high risk hpvs","volume":"5","author":"Uversky","year":"2006","journal-title":"J. Proteome Res."},{"key":"B79","doi-asserted-by":"publisher","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"Gromacs: fast, flexible, and free","volume":"26","author":"Van der Spoel","year":"2005","journal-title":"J. Comput. Chem."},{"key":"B80","doi-asserted-by":"publisher","first-page":"D326","DOI":"10.1093\/nar\/gkt960","article-title":"pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins","volume":"42","author":"Varadi","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"B81","doi-asserted-by":"publisher","first-page":"144504","DOI":"10.1063\/1.2056539","article-title":"Relation between the melting temperature and the temperature of maximum density for the most common models of water","volume":"123","author":"Vega","year":"2005","journal-title":"J. Chem. Phys."},{"key":"B82","doi-asserted-by":"publisher","first-page":"10507","DOI":"10.1021\/ja902528f","article-title":"Determination of multicomponent protein structures in solution using global orientation and shape restraints","volume":"131","author":"Wang","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"B83","doi-asserted-by":"publisher","first-page":"9956","DOI":"10.1021\/jp403802c","article-title":"Systematic improvement of a classical molecular model of water","volume":"117","author":"Wang","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"B84","doi-asserted-by":"publisher","first-page":"1885","DOI":"10.1021\/jz500737m","article-title":"Building force fields: an automatic, systematic, and reproducible approach","volume":"5","author":"Wang","year":"2014","journal-title":"J. Phys. Chem. Lett."},{"key":"B85","doi-asserted-by":"publisher","first-page":"5762","DOI":"10.1073\/pnas.0801353105","article-title":"Structure of tumor suppressor p53 and its intrinsically disordered n-terminal transactivation domain","volume":"105","author":"Wells","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B86","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1634\/theoncologist.2009-0009","article-title":"The role of src in solid tumors","volume":"14","author":"Wheeler","year":"2009","journal-title":"Oncologist"},{"key":"B87","doi-asserted-by":"crossref","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":"B88","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1038\/nrm3920","article-title":"Intrinsically disordered proteins in cellular signaling and regulation","volume":"16","author":"Wright","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B89","doi-asserted-by":"publisher","first-page":"2162","DOI":"10.1016\/j.str.2013.09.014","article-title":"Phosphorylation drives a dynamic switch in serine\/arginine-rich proteins","volume":"21","author":"Xiang","year":"2013","journal-title":"Structure"},{"key":"B90","doi-asserted-by":"publisher","first-page":"15757","DOI":"10.1073\/pnas.1004569107","article-title":"Multidomain assembled states of hck tyrosine kinase in solution","volume":"107","author":"Yang","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."}],"container-title":["Frontiers in Molecular Biosciences"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/article\/10.3389\/fmolb.2019.00064\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,20]],"date-time":"2019-09-20T08:43:13Z","timestamp":1568968993000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/article\/10.3389\/fmolb.2019.00064\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,8,13]]},"references-count":90,"alternative-id":["10.3389\/fmolb.2019.00064"],"URL":"https:\/\/doi.org\/10.3389\/fmolb.2019.00064","relation":{},"ISSN":["2296-889X"],"issn-type":[{"value":"2296-889X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,8,13]]},"article-number":"64"}}