M. Alborghetti, A. Furlan, J. Silva, P. Leme, A. Torriani et al., Human FEZ1 Protein Forms a Disulfide Bond Mediated Dimer: Implications for Cargo Transport, Journal of Proteome Research, vol.9, issue.9, pp.4595-4603, 2010.
DOI : 10.1021/pr100314q

S. Doniach, Changes in Biomolecular Conformation Seen by Small Angle X-ray Scattering, Chemical Reviews, vol.101, issue.6, pp.1763-1778, 2001.
DOI : 10.1021/cr990071k

L. Dougan, J. Li, C. Badilla, B. Berne, and J. Fernandez, Single homopolypeptide chains collapse into mechanically rigid conformations, Proceedings of the National Academy of Sciences, vol.292, issue.5521, pp.12605-12610, 2009.
DOI : 10.1126/science.292.5521.1552

URL : http://www.pnas.org/content/106/31/12605.full.pdf

A. Dunker, M. Cortese, P. Romero, L. Iakoucheva, and V. Uversky, Flexible nets. The roles of intrinsic disorder in protein interaction networks, FEBS Journal, vol.14, issue.20, pp.5129-5148, 2005.
DOI : 10.1088/2058-7058/14/7/32

H. Dyson and P. Wright, Unfolded Proteins and Protein Folding Studied by NMR, Chemical Reviews, vol.104, issue.8, pp.3607-3622, 2004.
DOI : 10.1021/cr030403s

D. Eliezer, Biophysical characterization of intrinsically disordered proteins, Current Opinion in Structural Biology, vol.19, issue.1, pp.23-30, 2009.
DOI : 10.1016/j.sbi.2008.12.004

A. Emperador, P. Sfriso, M. Villarreal, J. Gelpí, and M. Orozco, PACSAB: Coarse-Grained Force Field for the Study of Protein???Protein Interactions and Conformational Sampling in Multiprotein Systems, Journal of Chemical Theory and Computation, vol.11, issue.12, pp.5929-5938, 2015.
DOI : 10.1021/acs.jctc.5b00660

L. Feigin and D. Svergun, Structure analysis by small-­?angle X-­?ray and neutron scattering, 1987.
DOI : 10.1007/978-1-4757-6624-0

M. Krzeminski, J. Marsh, C. Neale, W. Choy, and J. Forman-­?kay, Characterization of disordered proteins with ENSEMBLE, Bioinformatics, vol.29, issue.3, pp.398-399, 2013.
DOI : 10.1093/bioinformatics/bts701

T. Huang, Structural analysis of poly-­?SUMO chain recognition by the RNF4-­?SIMs domain, Biochem J, vol.462, pp.53-65, 2014.

K. Lee and J. Chen, Multiscale enhanced sampling of intrinsically disordered protein conformations, Journal of Computational Chemistry, vol.23, issue.6, pp.550-557, 2016.
DOI : 10.1016/0021-9991(77)90098-5

J. Leguillou and J. Zinn-­?justin, -Vector Model in Three Dimensions from Field Theory, Physical Review Letters, vol.7, issue.2, pp.95-98, 1977.
DOI : 10.1103/PhysRevA.7.2145

Z. Lens, F. Dewitte, D. Monté, J. Baert, C. Bompard et al., Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1, Biochemical and Biophysical Research Communications, vol.399, issue.1, pp.104-110, 2010.
DOI : 10.1016/j.bbrc.2010.07.049

S. Lenton, T. Seydel, T. Nylander, C. Holt, M. Härtlein et al., Dynamic footprint of sequestration in the molecular fluctuations of osteopontin, Journal of The Royal Society Interface, vol.10, issue.110, p.506, 2015.
DOI : 10.1016/j.actbio.2013.10.010

M. Levitt, Nature of the protein universe, Proceedings of the National Academy of Sciences, vol.51, issue.4, pp.11079-11084, 2009.
DOI : 10.1002/prot.10347

C. Leyrat, M. Jensen, E. Ribeiro, . Jr, F. Gérard et al., -binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient ??-helices, Protein Science, vol.25, issue.3, pp.542-556, 2011.
DOI : 10.1002/jcc.10420

J. Li, V. Uversky, and A. Fink, Conformational Behavior of Human ??-Synuclein is Modulated by Familial Parkinson???s Disease Point Mutations A30P and A53T, NeuroToxicology, vol.23, issue.4-5, pp.553-567, 2002.
DOI : 10.1016/S0161-813X(02)00066-9

K. Lindorff-larsen, S. Kristjansdottir, K. Teilum, W. Fieber, C. Dobson et al., Determination of an Ensemble of Structures Representing the Denatured State of the Bovine Acyl-Coenzyme A Binding Protein, Journal of the American Chemical Society, vol.126, issue.10, p.3291, 2004.
DOI : 10.1021/ja039250g

S. Longhi, V. Receveur-­?bréchot, D. Karlin, K. Johansson, H. Darbon et al., The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein, Journal of Biological Chemistry, vol.63, issue.20, pp.18638-18648, 2003.
DOI : 10.1084/jem.186.2.269

M. Louhivuori, K. Pääkkönen, K. Fredriksson, P. Permi, J. Lounila et al., On the Origin of Residual Dipolar Couplings from Denatured Proteins, Journal of the American Chemical Society, vol.125, issue.50, pp.15647-15650, 2003.
DOI : 10.1021/ja035427v

C. Marasini, L. Galeno, and O. Moran, A SAXS-based ensemble model of the native and phosphorylated regulatory domain of the CFTR, Cellular and Molecular Life Sciences, vol.1808, issue.5, pp.923-933, 2013.
DOI : 10.1016/j.bbamem.2010.08.012

E. Marcotte, M. Pellegrini, T. Yeates, and D. Eisenberg, A census of protein repeats, Journal of Molecular Biology, vol.293, issue.1, pp.151-160, 1999.
DOI : 10.1006/jmbi.1999.3136

J. Marsh, C. Neale, F. Jack, W. Choy, A. Lee et al., Improved Structural Characterizations of the drkN SH3 Domain Unfolded State Suggest a Compact Ensemble with Native-like and Non-native Structure, Journal of Molecular Biology, vol.367, issue.5, pp.1494-1510, 2007.
DOI : 10.1016/j.jmb.2007.01.038

J. Marsh, J. Baker, M. Tollinger, and J. Forman-­?kay, Calculation of Residual Dipolar Couplings from Disordered State Ensembles Using Local Alignment, Journal of the American Chemical Society, vol.130, issue.25, pp.7804-7805, 2008.
DOI : 10.1021/ja802220c

J. Marsh, B. Dancheck, M. Ragusa, M. Allaire, J. Forman-­?kay et al., Structural Diversity in Free and Bound States of Intrinsically Disordered Protein Phosphatase 1 Regulators, Structure, vol.18, issue.9, pp.1094-1103, 2010.
DOI : 10.1016/j.str.2010.05.015

S. Meier, S. Grzesiek, and M. Blackledge, Mapping the Conformational Landscape of Urea-Denatured Ubiquitin Using Residual Dipolar Couplings, Journal of the American Chemical Society, vol.129, issue.31, pp.9799-9807, 2007.
DOI : 10.1021/ja0724339

H. Mertens and D. Svergun, Structural characterization of proteins and complexes using small-angle X-ray solution scattering, Journal of Structural Biology, vol.172, issue.1, pp.128-141, 2010.
DOI : 10.1016/j.jsb.2010.06.012

B. Rozycki, Y. Kim, and G. Hummer, SAXS Ensemble Refinement of ESCRT-III CHMP3 Conformational Transitions, Structure, vol.19, issue.1, pp.109-116, 2011.
DOI : 10.1016/j.str.2010.10.006

S. Ruskamo, M. Chukhlieb, J. Vahokoski, S. Bhargav, F. Liang et al., Juxtanodin is an intrinsically disordered F-actin-binding protein, Scientific Reports, vol.24, issue.1, p.899, 2012.
DOI : 10.1016/S0091-679X(08)60661-5

URL : http://www.nature.com/articles/srep00899.pdf

M. Schwalbe, V. Ozenne, S. Bibow, M. Jaremko, L. Jaremko et al., Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ??-Synuclein in Solution from NMR and Small Angle Scattering, Structure, vol.22, issue.2, pp.238-249, 2014.
DOI : 10.1016/j.str.2013.10.020

URL : https://hal.archives-ouvertes.fr/hal-01131132

S. Schwarzinger, G. Kroon, T. Foss, P. Wright, and H. Dyson, Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView, Journal of Biomolecular NMR, vol.18, issue.1, pp.43-48, 2000.
DOI : 10.1023/A:1008386816521

S. Shell, C. Putnam, and R. Kolodner, The N Terminus of Saccharomyces cerevisiae Msh6 Is an Unstructured Tether to PCNA, Molecular Cell, vol.26, issue.4, pp.565-578, 2007.
DOI : 10.1016/j.molcel.2007.04.024

A. Shkumatov, S. Chinnathambi, E. Mandelkow, and D. Svergun, Structural memory of natively unfolded tau protein detected by small-angle X-ray scattering, Proteins: Structure, Function, and Bioinformatics, vol.28, issue.6 Pt 2, pp.2122-2131, 2011.
DOI : 10.1007/s10930-009-9201-4

N. Sibille and P. Bernadó, Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS, Biochemical Society Transactions, vol.80, issue.5, pp.955-962, 2012.
DOI : 10.1021/ja012750u

A. Stadler, L. Stingaciu, A. Radulescu, O. Holderer, M. Monkenbusch et al., Internal Nanosecond Dynamics in the Intrinsically Disordered Myelin Basic Protein, Journal of the American Chemical Society, vol.136, issue.19, pp.6987-6994, 2014.
DOI : 10.1021/ja502343b

C. Stanley, T. Perevozchikova, and V. Berthelier, Structural Formation of Huntingtin Exon 1 Aggregates Probed by Small-Angle Neutron Scattering, Biophysical Journal, vol.100, issue.10, pp.2504-2512, 2011.
DOI : 10.1016/j.bpj.2011.04.022

Y. Sterckx, A. Volkov, W. Vranken, J. Kragelj, M. Jensen et al., Small-Angle X-Ray Scattering- and Nuclear Magnetic Resonance-Derived Conformational Ensemble of the Highly Flexible Antitoxin PaaA2, Structure, vol.22, issue.6, pp.854-865, 2014.
DOI : 10.1016/j.str.2014.03.012

URL : https://hal.archives-ouvertes.fr/hal-01131143

K. Stott, M. Watson, F. Howe, J. Grossmann, and J. Thomas, Tail-Mediated Collapse of HMGB1 Is Dynamic and Occurs via Differential Binding of the Acidic Tail to the A and B Domains, Journal of Molecular Biology, vol.403, issue.5, pp.706-722, 2010.
DOI : 10.1016/j.jmb.2010.07.045

M. Stumpe and H. Grubmüller, Interaction of Urea with Amino Acids:?? Implications for Urea-Induced Protein Denaturation, Journal of the American Chemical Society, vol.129, issue.51, pp.16126-16131, 2007.
DOI : 10.1021/ja076216j

D. Svergun and M. Koch, Small-angle scattering studies of biological macromolecules in solution, Reports on Progress in Physics, vol.66, issue.10, pp.1735-1782, 2003.
DOI : 10.1088/0034-4885/66/10/R05

K. Tamiola, B. Acar, and F. Mulder, Sequence-Specific Random Coil Chemical Shifts of Intrinsically Disordered Proteins, Journal of the American Chemical Society, vol.132, issue.51, pp.18000-18003, 2010.
DOI : 10.1021/ja105656t

T. Trakawa and S. Takada, Multiscale Ensemble Modeling of Intrinsically Disordered Proteins: p53 N-Terminal Domain, Biophysical Journal, vol.101, issue.6, pp.1450-1458, 2011.
DOI : 10.1016/j.bpj.2011.08.003

D. Wishart and B. Sykes, The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data, Journal of Biomolecular NMR, vol.4, issue.2, pp.171-180, 1994.
DOI : 10.1007/BF00175245

J. Wootton and S. Federhen, Statistics of local complexity in amino acid sequences and sequence databases, Computers & Chemistry, vol.17, issue.2, pp.149-163, 1993.
DOI : 10.1016/0097-8485(93)85006-X

P. Wright and H. Dyson, Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, Journal of Molecular Biology, vol.293, issue.2, pp.321-331, 1999.
DOI : 10.1006/jmbi.1999.3110

URL : http://www.chem.umass.edu/~cmartin/Courses/BioStruct/F2000/DysonWrightUnstruct.pdf

P. Wright and H. Dyson, Intrinsically disordered proteins in cellular signalling and regulation, Nature Reviews Molecular Cell Biology, vol.106, issue.1, pp.18-29, 2015.
DOI : 10.1073/pnas.0906770106

URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4405151/pdf

K. Wu, D. Weinstock, C. Narayanan, R. Levy, and J. Baum, Structural Reorganization of ??-Synuclein at Low pH Observed by NMR and REMD Simulations, Journal of Molecular Biology, vol.391, issue.4, p.784, 2009.
DOI : 10.1016/j.jmb.2009.06.063

C. Yang, M. Van-der-woerd, U. Muthurajan, J. Hansen, and K. Luger, Biophysical analysis and small-angle X-ray scattering-derived structures of MeCP2???nucleosome complexes, Nucleic Acids Research, vol.39, issue.10, pp.4122-4135, 2011.
DOI : 10.1093/nar/gkr005

S. Yang, L. Blachowicz, L. Makowski, and B. Roux, Multidomain assembled states of Hck tyrosine kinase in solution, Proceedings of the National Academy of Sciences, vol.13, issue.12, pp.15757-15762, 2010.
DOI : 10.1016/j.str.2005.08.009

S. Yang, Methods for SAXS-Based Structure Determination of Biomolecular Complexes, Advanced Materials, vol.334, issue.2, 2014.
DOI : 10.1126/science.1208351

G. Zerze, C. Miller, D. Granata, and J. Mittal, Free Energy Surface of an Intrinsically Disordered Protein: Comparison between Temperature Replica Exchange Molecular Dynamics and Bias-Exchange Metadynamics, Journal of Chemical Theory and Computation, vol.11, issue.6, pp.2776-2782, 2015.
DOI : 10.1021/acs.jctc.5b00047

C. Zhou, F. Confalonieri, M. Jacquet, R. Perasso, Z. Li et al., Silk fibroin: Structural implications of a remarkable amino acid sequence, Proteins: Structure, Function, and Genetics, vol.24, issue.2, pp.119-122, 2001.
DOI : 10.1016/S0141-8130(98)00080-4