{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T03:40:01Z","timestamp":1785210001056,"version":"3.55.0"},"reference-count":58,"publisher":"Oxford University Press (OUP)","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2012,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: Intrinsically disordered proteins (IDPs) represent a significant fraction of the human proteome. The classical structure function paradigm that has successfully underpinned our understanding of molecular biology breaks down when considering proteins that have no stable tertiary structure in their functional form. One convenient approach is to describe the protein in terms of an equilibrium of rapidly inter-converting conformers. Currently, tools to generate such ensemble descriptions are extremely rare, and poorly adapted to the prediction of experimental data.<\/jats:p>\n               <jats:p>Results: We present flexible-meccano\u2014a highly efficient algorithm that generates ensembles of molecules, on the basis of amino acid-specific conformational potentials and volume exclusion. Conformational sampling depends uniquely on the primary sequence, with the possibility of introducing additional local or long-range conformational propensities at an amino acid-specific resolution. The algorithm can also be used to calculate expected values of experimental parameters measured at atomic or molecular resolution, such as nuclear magnetic resonance (NMR) and small angle scattering, respectively. We envisage that flexible-meccano will be useful for researchers who wish to compare experimental data with those expected from a fully disordered protein, researchers who see experimental evidence of deviation from \u2018random coil\u2019 behaviour in their protein, or researchers who are interested in working with a broad ensemble of conformers representing the flexibility of the IDP of interest.<\/jats:p>\n               <jats:p>Availability: A fully documented multi-platform executable is provided, with examples, at http:\/\/www.ibs.fr\/science-213\/scientific-output\/software\/flexible-meccano\/<\/jats:p>\n               <jats:p>Contact: \u00a0martin.blackledge@ibs.fr<\/jats:p>","DOI":"10.1093\/bioinformatics\/bts172","type":"journal-article","created":{"date-parts":[[2012,5,21]],"date-time":"2012-05-21T06:03:24Z","timestamp":1337580204000},"page":"1463-1470","source":"Crossref","is-referenced-by-count":364,"title":["<i>Flexible-meccano:<\/i> a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables"],"prefix":"10.1093","volume":"28","author":[{"given":"Val\u00e9ry","family":"Ozenne","sequence":"first","affiliation":[{"name":"1 Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; CNRS; UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, 2Groupe Informatique pour les Scientifiques du Sud Est (GIPSE), IRTSV \/ Laboratoire Biologie \u00e0 Grande Echelle, CEA - INSERM U1038 - UJF, 17 avenue des Martyrs, 38054 Grenoble Cedex 9 and 3Centre de Biochimie Structurale, CNRS UMR 5048 - UM 1 - INSERM UMR 1054, 34090, Montpelier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fr\u00e9d\u00e9ric","family":"Bauer","sequence":"additional","affiliation":[{"name":"1 Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; CNRS; UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, 2Groupe Informatique pour les Scientifiques du Sud Est (GIPSE), IRTSV \/ Laboratoire Biologie \u00e0 Grande Echelle, CEA - INSERM U1038 - UJF, 17 avenue des Martyrs, 38054 Grenoble Cedex 9 and 3Centre de Biochimie Structurale, CNRS UMR 5048 - UM 1 - INSERM UMR 1054, 34090, Montpelier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lo\u00efc","family":"Salmon","sequence":"additional","affiliation":[{"name":"1 Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; 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CNRS; UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, 2Groupe Informatique pour les Scientifiques du Sud Est (GIPSE), IRTSV \/ Laboratoire Biologie \u00e0 Grande Echelle, CEA - INSERM U1038 - UJF, 17 avenue des Martyrs, 38054 Grenoble Cedex 9 and 3Centre de Biochimie Structurale, CNRS UMR 5048 - UM 1 - INSERM UMR 1054, 34090, Montpelier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9line","family":"Charavay","sequence":"additional","affiliation":[{"name":"1 Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; CNRS; UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, 2Groupe Informatique pour les Scientifiques du Sud Est (GIPSE), IRTSV \/ Laboratoire Biologie \u00e0 Grande Echelle, CEA - INSERM U1038 - UJF, 17 avenue des Martyrs, 38054 Grenoble Cedex 9 and 3Centre de Biochimie Structurale, CNRS UMR 5048 - UM 1 - INSERM UMR 1054, 34090, Montpelier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Blackledge","sequence":"additional","affiliation":[{"name":"1 Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; 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Biol."},{"key":"2023012512312849800_B21","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.sbi.2011.04.001","article-title":"Constructing ensembles for intrinsically disordered proteins","volume":"21","author":"Fisher","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2023012512312849800_B22","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1006\/jmbi.1997.0953","article-title":"Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures","volume":"268","author":"Gillespie","year":"1997","journal-title":"J. Mol. Biol."},{"key":"2023012512312849800_B23","doi-asserted-by":"crossref","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. 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Biol."},{"key":"2023012512312849800_B33","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1110\/ps.062465306","article-title":"Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation","volume":"15","author":"Marsh","year":"2006","journal-title":"Protein Sci."},{"key":"2023012512312849800_B34","doi-asserted-by":"crossref","first-page":"7804","DOI":"10.1021\/ja802220c","article-title":"Calculation of residual dipolar couplings from disordered state ensembles using local alignment","volume":"130","author":"Marsh","year":"2008","journal-title":"J. Am. Chem. 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Mol. Biol."},{"key":"2023012512312849800_B39","doi-asserted-by":"crossref","first-page":"5235","DOI":"10.1021\/ja0690159","article-title":"Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation","volume":"129","author":"Mukrasch","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"2023012512312849800_B40","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1023\/A:1023812930288","article-title":"Rapid and accurate calculation of protein1H13C and15N chemical shifts","volume":"26","author":"Neal","year":"2003","journal-title":"J. Biomol. NMR"},{"key":"2023012512312849800_B41","doi-asserted-by":"crossref","first-page":"17908","DOI":"10.1021\/ja9069024","article-title":"Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings","volume":"131","author":"Nodet","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"2023012512312849800_B42","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/0022-2836(84)90035-4","article-title":"Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure","volume":"180","author":"Pardi","year":"1984","journal-title":"J. Mol. Biol."},{"key":"2023012512312849800_B43","doi-asserted-by":"crossref","first-page":"4154","DOI":"10.1002\/anie.200900476","article-title":"Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin","volume":"48","author":"Salmon","year":"2009","journal-title":"Angew. Chem. Int. Ed. 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Soc."},{"key":"2023012512312849800_B47","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/s10858-007-9166-6","article-title":"Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology","volume":"38","author":"Shen","year":"2007","journal-title":"J. Biomol. NMR"},{"key":"2023012512312849800_B48","doi-asserted-by":"crossref","first-page":"4685","DOI":"10.1073\/pnas.0800256105","article-title":"Consistent blind protein structure generation from NMR chemical shift data","volume":"105","author":"Shen","year":"2008","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2023012512312849800_B49","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1006\/jmbi.1996.0041","article-title":"Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations","volume":"255","author":"Smith","year":"1996","journal-title":"J. Mol. Biol."},{"key":"2023012512312849800_B50","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1107\/S0021889895007047","article-title":"CRYSOL - A 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":"2023012512312849800_B51","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/S0968-0004(02)02169-2","article-title":"Intrinsically unstructured proteins","volume":"27","author":"Tompa","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"2023012512312849800_B52","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.sbi.2011.03.012","article-title":"Unstructural biology coming of age","volume":"21","author":"Tompa","year":"2011","journal-title":"Curr. Opin. Struct. 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