A. K. Dunker, What???s in a name? Why these proteins are intrinsically disordered, Intrinsically Disordered Proteins, vol.80, issue.1, p.24157, 2013.
DOI : 10.1016/j.bbapap.2012.12.008

URL : http://www.tandfonline.com/doi/pdf/10.4161/idp.24157?needAccess=true

V. N. Uversky, Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs, Intrinsically Disordered Proteins, vol.11, issue.20, pp.1-42, 2014.
DOI : 10.1007/s00018-011-0859-3

URL : http://europepmc.org/articles/pmc5314882?pdf=render

P. E. Wright and H. J. 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

J. Habchi, P. Tompa, S. Longhi, and V. N. Uversky, Introducing Protein Intrinsic Disorder, Chemical Reviews, vol.114, issue.13, pp.6561-6588, 2014.
DOI : 10.1021/cr400514h

URL : http://real.mtak.hu/19536/1/Habchi_et_al_2014_Chem_Rev_u_142547.424768.pdf

A. Campen, TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder, Protein & Peptide Letters, vol.15, issue.9, p.956, 2008.
DOI : 10.2174/092986608785849164

URL : http://europepmc.org/articles/pmc2676888?pdf=render

L. M. Iakoucheva, The importance of intrinsic disorder for protein phosphorylation, Nucleic Acids Research, vol.32, issue.3, pp.1037-1049, 2004.
DOI : 10.1093/nar/gkh253

URL : https://academic.oup.com/nar/article-pdf/32/3/1037/9489921/gkh253.pdf

V. Mathura, The protein non-folding problem: amino acid determinants of intrinsic order and disorder, Paper presented at Pacific Symposium on Biocomputing: Disorder and flexibility in protein structure and function, 2001.

P. Tompa, Intrinsically unstructured proteins, Trends in Biochemical Sciences, vol.27, issue.10, pp.527-533, 2002.
DOI : 10.1016/S0968-0004(02)02169-2

V. N. Uversky, What does it mean to be natively unfolded?, European Journal of Biochemistry, vol.39, issue.1, pp.2-12, 2002.
DOI : 10.1021/bi992770x

URL : http://onlinelibrary.wiley.com/doi/10.1046/j.0014-2956.2001.02649.x/pdf

J. J. Ward, J. S. Sodhi, L. J. Mcguffin, B. F. Buxton, and D. T. Jones, Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life, Journal of Molecular Biology, vol.337, issue.3, pp.635-645, 2004.
DOI : 10.1016/j.jmb.2004.02.002

K. Yegambaram, E. Bulloch, and R. Kingston, Protein domain definition should allow for conditional disorder, Protein Science, vol.25, issue.11, pp.1502-1518, 2013.
DOI : 10.1002/jcc.20084

URL : http://onlinelibrary.wiley.com/doi/10.1002/pro.2336/pdf

A. Kurotani, Correlations between predicted protein disorder and post-translational modifications in plants, Bioinformatics, vol.3, issue.8, pp.1095-1103, 2014.
DOI : 10.3389/fpls.2012.00186

URL : https://academic.oup.com/bioinformatics/article-pdf/30/8/1095/17141676/btt762.pdf

U. Jakob, R. Kriwacki, and V. N. Uversky, Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function, Chemical Reviews, vol.114, issue.13, pp.6779-6805, 2014.
DOI : 10.1021/cr400459c

URL : http://europepmc.org/articles/pmc4090257?pdf=render

H. Wang, Reveals Complex Organellar Phosphorylation in the Flagella and Thylakoid Membrane, Molecular & Cellular Proteomics, vol.4, issue.9, pp.2337-2353, 2014.
DOI : 10.1074/jbc.M505729200

URL : http://www.mcponline.org/content/13/9/2337.full.pdf

H. J. Dyson and P. Wright, Intrinsically unstructured proteins and their functions, Nature Reviews Molecular Cell Biology, vol.278, issue.3, pp.197-208, 2005.
DOI : 10.1074/jbc.M210385200

V. N. Uversky, C. J. Oldfield, and A. K. Dunker, Concept, Annual Review of Biophysics, vol.37, issue.1, pp.215-246, 2008.
DOI : 10.1146/annurev.biophys.37.032807.125924

B. Xue, A. K. Dunker, and V. N. Uversky, Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life, Journal of Biomolecular Structure and Dynamics, vol.15, issue.1, pp.137-149, 2012.
DOI : 10.1016/0968-0004(90)90068-M

E. Schad, P. Tompa, and H. Hegyi, The relationship between proteome size, structural disorder and organism complexity, Genome Biology, vol.12, issue.12, pp.1-13, 2011.
DOI : 10.1093/nar/gkq973

URL : https://genomebiology.biomedcentral.com/track/pdf/10.1186/gb-2011-12-12-r120?site=genomebiology.biomedcentral.com

Z. Peng, Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life, Cellular and Molecular Life Sciences, vol.296, issue.5568, pp.137-151, 2015.
DOI : 10.1126/science.1068696

I. Yruela, Plant development regulation: Overview and perspectives, Journal of Plant Physiology, vol.182, pp.62-78, 2015.
DOI : 10.1016/j.jplph.2015.05.006

URL : https://digital.csic.es/bitstream/10261/116180/1/YruelaI_JPlantPhys_2015.pdf

I. Yruela, C. J. Oldfield, K. J. Niklas, and A. K. Dunker, Evidence for a Strong Correlation Between Transcription Factor Protein Disorder and Organismic Complexity, Genome Biology and Evolution, vol.43, issue.D1, pp.1248-1265, 2017.
DOI : 10.1093/nar/gku887

URL : https://academic.oup.com/gbe/article-pdf/9/5/1248/19511354/evx073.pdf

K. J. Niklas, S. E. Bondos, A. K. Dunker, and S. A. Newman, Rethinking gene regulatory networks in light of alternative splicing, intrinsically disordered protein domains, and post-translational modifications, Frontiers in Cell and Developmental Biology, vol.2011, issue.374, pp.1-13, 2015.
DOI : 10.1155/2011/616451

URL : https://www.frontiersin.org/articles/10.3389/fcell.2015.00008/pdf

A. K. Dunker, S. E. Bondos, F. Huang, and C. J. Oldfield, Intrinsically disordered proteins and multicellular organisms, Seminars in Cell & Developmental Biology, vol.37, pp.44-55, 2015.
DOI : 10.1016/j.semcdb.2014.09.025

D. Piovesan, DisProt 7.0: a major update of the database of disordered proteins, Nucleic Acids Research, vol.25, issue.D1, pp.219-227, 2017.
DOI : 10.1021/bi012159+

M. Sickmeier, DisProt: the Database of Disordered Proteins, Nucleic Acids Research, vol.35, issue.Database, pp.786-793, 2007.
DOI : 10.1093/nar/gkl893

URL : https://academic.oup.com/nar/article-pdf/35/suppl_1/D786/3862071/gkl893.pdf

D. Kovacs, E. Kalmar, Z. Torok, and P. Tompa, Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins, PLANT PHYSIOLOGY, vol.147, issue.1, pp.381-390, 2008.
DOI : 10.1104/pp.108.118208

URL : http://www.plantphysiol.org/content/plantphysiol/147/1/381.full.pdf

P. Tompa and D. Kovacs, Intrinsically disordered chaperones in plants and animalsThis paper is one of a selection of papers published in this special issue entitled ???Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting ??? Protein Folding: Principles and Diseases??? and has undergone the Journal's usual peer review process., Biochemistry and Cell Biology, vol.25, issue.10, pp.167-174, 2010.
DOI : 10.1016/S0301-4622(96)02222-3

X. Sun, E. H. Rikkerink, W. T. Jones, and V. N. Uversky, Multifarious Roles of Intrinsic Disorder in Proteins Illustrate Its Broad Impact on Plant Biology, The Plant Cell, vol.25, issue.1, pp.38-55, 2013.
DOI : 10.1105/tpc.112.106062

URL : http://www.plantcell.org/content/plantcell/25/1/38.full.pdf

X. Sun, A functionally required unfoldome from the plant kingdom: intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development, Plant Molecular Biology, vol.108, issue.3, pp.205-223, 2011.
DOI : 10.1073/pnas.1012232108

F. Pazos, N. Pietrosemoli, J. A. García-martín, and R. Solano, Protein intrinsic disorder in plants, Frontiers in Plant Science, vol.4, pp.1-5, 2013.
DOI : 10.3389/fpls.2013.00363

URL : http://journal.frontiersin.org/article/10.3389/fpls.2013.00363/pdf

A. A. Covarrubias, C. L. Cuevas-velazquez, P. S. Romero-pérez, D. F. Rendón-luna, and C. Chater, Structural disorder in plant proteins: where plasticity meets sessility, Cellular and Molecular Life Sciences, vol.14, issue.9, pp.3119-3147, 2017.
DOI : 10.1038/nrc3800

N. Pietrosemoli, J. A. García-martín, R. Solano, and F. Pazos, Genome-Wide Analysis of Protein Disorder in Arabidopsis thaliana: Implications for Plant Environmental Adaptation, PLoS ONE, vol.6, issue.2, p.55524, 2013.
DOI : 10.1371/journal.pone.0055524.s004

URL : https://doi.org/10.1371/journal.pone.0055524

M. Vincent and S. Schnell, A collection of intrinsic disorder characterizations from eukaryotic proteomes, Scientific Data, vol.3, pp.1-9, 2016.
DOI : 10.1073/pnas.1304749110

URL : http://www.nature.com/articles/sdata201645.pdf

V. Csizmók, Z. Dosztányi, I. Simon, and P. Tompa, Towards Proteomic Approaches for the Identification of Structural Disorder, Current Protein & Peptide Science, vol.8, issue.2, pp.173-179, 2007.
DOI : 10.2174/138920307780363479

M. S. Cortese, J. P. Baird, V. N. Uversky, and A. K. Dunker, Uncovering the Unfoldome:?? Enriching Cell Extracts for Unstructured Proteins by Acid Treatment, Journal of Proteome Research, vol.4, issue.5, pp.1610-1618, 2005.
DOI : 10.1021/pr050119c

C. A. Galea, Proteomic Studies of the Intrinsically Unstructured Mammalian Proteome, Journal of Proteome Research, vol.5, issue.10, pp.2839-2848, 2006.
DOI : 10.1021/pr060328c

S. Irar, E. Oliveira, and A. Goday, Towards the identification of late-embryogenic-abundant phosphoproteome in Arabidopsis by 2-DE and MS, PROTEOMICS, vol.7, issue.S1, pp.175-185, 2006.
DOI : 10.1007/978-94-011-4431-5_32

J. Rochaix, as the Photosynthetic Yeast, Annual Review of Genetics, vol.29, issue.1, pp.209-230, 1995.
DOI : 10.1146/annurev.ge.29.120195.001233

L. Avilan, is intermediate between a chlorophyte and a diatom, European Journal of Phycology, vol.251, issue.3, pp.207-215, 2012.
DOI : 10.1111/j.1432-1033.1976.tb11025.x

URL : http://www.tandfonline.com/doi/pdf/10.1080/09670262.2012.687459?needAccess=true

E. Graciet, The Small Protein CP12:?? A Protein Linker for Supramolecular Complex Assembly, Biochemistry, vol.42, issue.27, pp.8163-8170, 2003.
DOI : 10.1021/bi034474x

URL : http://eprints.maynoothuniversity.ie/7436/1/EG-Small-protein-2003.pdf

H. Launay, Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state, Biochemical and Biophysical Research Communications, vol.477, issue.1, pp.20-26, 2016.
DOI : 10.1016/j.bbrc.2016.06.014

URL : https://hal.archives-ouvertes.fr/hal-01430932

S. B. Moparthi, FRET analysis of CP12 structural interplay by GAPDH and PRK, Biochemical and Biophysical Research Communications, vol.458, issue.3, pp.488-493, 2015.
DOI : 10.1016/j.bbrc.2015.01.135

URL : https://hal.archives-ouvertes.fr/hal-01429065

B. Gontero and S. C. Maberly, An intrinsically disordered protein, CP12: jack of all trades and master of the Calvin cycle, Biochemical Society Transactions, vol.725, issue.5, pp.995-999, 2012.
DOI : 10.1042/BJ20082004

URL : http://www.biochemsoctrans.org/content/ppbiost/40/5/995.full.pdf

J. Erales, S. Lignon, and B. Gontero, , a Permanent Specific ???Chaperone-like??? Protein of Glyceraldehyde-3-phosphate Dehydrogenase, Journal of Biological Chemistry, vol.1784, issue.19, pp.12735-12744, 2009.
DOI : 10.1086/430799

URL : http://www.jbc.org/content/284/19/12735.full.pdf

A. Delobel, Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: a possible regulatory role within a PRK/GAPDH/CP12 complex, Rapid Communications in Mass Spectrometry, vol.117, issue.22, pp.3379-3388, 2005.
DOI : 10.1016/j.bbapap.2003.12.008

URL : https://hal.archives-ouvertes.fr/hal-00015671

L. C. Mackinder, A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle, Proceedings of the National Academy of Sciences, vol.221, issue.3, pp.5958-5963, 2016.
DOI : 10.1006/jmbi.2000.4315

URL : http://www.pnas.org/content/113/21/5958.full.pdf

F. Meng, V. Uversky, and L. Kurgan, Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions, Cellular and Molecular Life Sciences, vol.42, issue.6, pp.3069-3090, 2017.
DOI : 10.1042/BST20140214

A. Bah and J. D. Forman-kay, Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications, Journal of Biological Chemistry, vol.3, issue.13, pp.6696-6705, 2016.
DOI : 10.1016/j.cbpa.2003.12.009

URL : http://europepmc.org/articles/pmc4807257?pdf=render

C. Haynes and L. M. Iakoucheva, Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins, Nucleic Acids Research, vol.34, issue.1, pp.305-312, 2006.
DOI : 10.1093/nar/gkj424

URL : https://academic.oup.com/nar/article-pdf/34/1/305/7128710/gkj424.pdf

J. R. Sanford and J. P. Bruzik, Developmental regulation of SR protein phosphorylation and activity, Genes & Development, vol.13, issue.12, pp.1513-1518, 1999.
DOI : 10.1101/gad.13.12.1513

URL : http://genesdev.cshlp.org/content/13/12/1513.full.pdf

E. G. Werth, via sequential enrichment and quantitative proteomics, The Plant Journal, vol.27, issue.2, pp.416-426, 2017.
DOI : 10.1002/mas.21447

A. Kurotani and T. Sakurai, In Silico Analysis of Correlations between Protein Disorder and Post-Translational Modifications in Algae, International Journal of Molecular Sciences, vol.8, issue.8, pp.19812-19835, 2015.
DOI : 10.1093/pcp/pcs184

URL : http://www.mdpi.com/1422-0067/16/8/19812/pdf

I. Yruela and B. Contreras-moreira, Protein disorder in plants: a view from the chloroplast, BMC Plant Biology, vol.12, issue.1, pp.165-176, 2012.
DOI : 10.1073/pnas.0709856104

URL : https://bmcplantbiol.biomedcentral.com/track/pdf/10.1186/1471-2229-12-165?site=bmcplantbiol.biomedcentral.com

D. Botstein, Gene Ontology: tool for the unification of biology, Nat Genet, vol.25, pp.25-29, 2000.

I. Yruela and B. Contreras-moreira, Genetic recombination is associated with intrinsic disorder in plant proteomes, BMC Genomics, vol.14, issue.1, pp.772-781, 2013.
DOI : 10.1186/1471-2164-14-772

URL : https://bmcgenomics.biomedcentral.com/track/pdf/10.1186/1471-2164-14-772?site=bmcgenomics.biomedcentral.com

J. C. Bardwell and U. Jakob, Conditional disorder in chaperone action, Trends in Biochemical Sciences, vol.37, issue.12, pp.517-525, 2012.
DOI : 10.1016/j.tibs.2012.08.006

URL : http://europepmc.org/articles/pmc3508372?pdf=render

C. M. Cremers, D. Reichmann, J. Hausmann, M. Ilbert, and U. Jakob, Unfolding of Metastable Linker Region Is at the Core of Hsp33 Activation as a Redox-regulated Chaperone, Journal of Biological Chemistry, vol.8, issue.15, pp.11243-11251, 2010.
DOI : 10.1016/j.bbrc.2007.04.184

URL : https://hal.archives-ouvertes.fr/hal-00677454

M. Ilbert, The redox-switch domain of Hsp33 functions as dual stress sensor, Nature Structural & Molecular Biology, vol.18, issue.6, pp.556-563, 2007.
DOI : 10.1038/nsmb1244

URL : http://europepmc.org/articles/pmc2782886?pdf=render

D. Reichmann, Order out of Disorder: Working Cycle of an Intrinsically Unfolded Chaperone, Cell, vol.148, issue.5, pp.947-957, 2012.
DOI : 10.1016/j.cell.2012.01.045

URL : https://doi.org/10.1016/j.cell.2012.01.045

N. Segal and M. Shapira, HSP33 in eukaryotes - an evolutionary tale of a chaperone adapted to photosynthetic organisms, The Plant Journal, vol.32, issue.5, pp.850-860, 2015.
DOI : 10.1093/nar/gnh110

J. C. Borges, T. V. Seraphim, P. R. Dores-silva, and L. R. Barbosa, A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering, Biophysical Reviews, vol.83, issue.8, pp.107-120, 2016.
DOI : 10.1139/o05-158

URL : http://europepmc.org/articles/pmc5425780?pdf=render

O. Genest, J. R. Hoskins, J. L. Camberg, S. M. Doyle, and S. Wickner, Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling, Proceedings of the National Academy of Sciences, vol.106, issue.26, pp.8206-8211, 2011.
DOI : 10.1073/pnas.0904886106

URL : http://www.pnas.org/content/108/20/8206.full.pdf

O. Genest, J. R. Hoskins, A. N. Kravats, S. M. Doyle, and S. Wickner, Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling, Journal of Molecular Biology, vol.427, issue.24, pp.3877-3889, 2015.
DOI : 10.1016/j.jmb.2015.10.010

URL : https://hal.archives-ouvertes.fr/hal-01432234

M. V. Beligni, K. Yamaguchi, and S. P. Mayfield, The translational apparatus of Chlamydomonas reinhardtii chloroplast, Photosynthesis Research, vol.96, issue.3, pp.315-325, 2004.
DOI : 10.1016/0167-4781(90)90058-A

J. Christodoulou, Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes, Proceedings of the National Academy of Sciences, vol.14, issue.1, pp.10949-10954, 2004.
DOI : 10.1016/S1097-2765(04)00179-0

URL : http://www.pnas.org/content/101/30/10949.full.pdf

J. C. Hansen, X. Lu, E. D. Ross, and R. W. Woody, Intrinsic Protein Disorder, Amino Acid Composition, and Histone Terminal Domains, Journal of Biological Chemistry, vol.281, issue.4, pp.1853-1856, 2006.
DOI : 10.1128/MCB.25.17.7616-7624.2005

URL : http://www.jbc.org/content/281/4/1853.full.pdf

T. Lazar, Intrinsic protein disorder in histone lysine methylation, Biology Direct, vol.22, issue.1, pp.30-39, 2016.
DOI : 10.1002/bip.360221211

URL : https://biologydirect.biomedcentral.com/track/pdf/10.1186/s13062-016-0129-2?site=biologydirect.biomedcentral.com

Z. Peng, M. J. Mizianty, B. Xue, L. Kurgan, and V. N. Uversky, More than just tails: intrinsic disorder in histone proteins, Molecular BioSystems, vol.14, issue.Suppl. 9, pp.1886-1901, 2012.
DOI : 10.1016/0263-7855(96)00018-5

G. Liu and K. Huang, Phosphorylation regulates the disassembly of cilia, Science China Life Sciences, vol.17, issue.6, pp.621-623, 2015.
DOI : 10.1016/j.cub.2007.03.048

URL : https://link.springer.com/content/pdf/10.1007%2Fs11427-015-4874-8.pdf

D. Giudice and A. , by small-angle X-ray scattering analysis, Acta Crystallographica Section D Biological Crystallography, vol.185, issue.186, pp.2372-2385, 2015.
DOI : 10.1107/S1399004715018520/gi5001sup1.pdf

S. Fermani, Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly, Journal of Biological Chemistry, vol.271, issue.25, pp.21372-21383, 2012.
DOI : 10.1002/prot.340230412

URL : http://www.jbc.org/content/287/25/21372.full.pdf

L. Marri, In vitro characterization of Arabidopsis CP12 isoforms reveals common biochemical and molecular properties, Journal of Plant Physiology, vol.167, issue.12, pp.939-950, 2010.
DOI : 10.1016/j.jplph.2010.02.008

L. Avilan, B. Gontero, S. Lebreton, and J. Ricard, Memory and Imprinting Effects in Multienzyme Complexes. I. Isolation, Dissociation, and Reassociation of a Phosphoribulokinase-Glyceraldehyde-3-Phosphate Dehydrogenase Complex from Chlamydomonas Reinhardtii Chloroplasts, European Journal of Biochemistry, vol.107, issue.1, pp.78-84, 1997.
DOI : 10.1111/j.1432-1033.1997.t01-2-00085.x

S. Abdelkafi, Identification and biochemical characterization of a GDSL-motif carboxylester hydrolase from Carica papaya latex, Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, vol.1791, issue.11, pp.1048-1056, 2009.
DOI : 10.1016/j.bbalip.2009.06.002

K. Peng, OPTIMIZING LONG INTRINSIC DISORDER PREDICTORS WITH PROTEIN EVOLUTIONARY INFORMATION, Journal of Bioinformatics and Computational Biology, vol.10, issue.01, pp.35-60, 2005.
DOI : 10.1002/(SICI)1097-0134(19980215)30:3<228::AID-PROT2>3.0.CO;2-G

J. Prilusky, FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded, Bioinformatics, vol.36, issue.13, pp.3435-3438, 2005.
DOI : 10.1021/bi9627626

URL : https://academic.oup.com/bioinformatics/article-pdf/21/16/3435/571946/bti537.pdf

P. Radivojac, Intrinsic Disorder and Functional Proteomics, Biophysical Journal, vol.92, issue.5, pp.1439-1456, 2007.
DOI : 10.1529/biophysj.106.094045

URL : https://doi.org/10.1529/biophysj.106.094045

M. Tardif, PredAlgo: A New Subcellular Localization Prediction Tool Dedicated to Green Algae, Molecular Biology and Evolution, vol.3, issue.12, pp.3625-3639, 2012.
DOI : 10.1371/journal.pone.0001994

URL : https://hal.archives-ouvertes.fr/hal-00783004

S. S. Merchant, The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions, Science, vol.435, issue.7038, pp.245-250, 2007.
DOI : 10.1038/nature03481

URL : https://hal.archives-ouvertes.fr/hal-00198837

V. Vacic, V. N. Uversky, A. K. Dunker, and S. Lonardi, Composition Profiler: a tool for discovery and visualization of amino acid composition differences, BMC Bioinformatics, vol.8, issue.1, pp.1471-2105, 2007.
DOI : 10.1186/1471-2105-8-211

URL : https://bmcbioinformatics.biomedcentral.com/track/pdf/10.1186/1471-2105-8-211?site=bmcbioinformatics.biomedcentral.com

H. M. Berman, The Protein Data Bank, Nucleic Acids Research, vol.28, issue.1, pp.235-242, 2000.
DOI : 10.1093/nar/28.1.235