Abstract
Currently available computational tools, which are many, provide a researcher with the multitude of options for prediction of intrinsic disorder in a protein of interest and for finding at least some of its disorder-based functions. This chapter provides a highly subjective guideline on how not to be lost in the “dark forest” of available tools for the analysis of intrinsic disorder. By no means it gives a unique pathway through this forest, but simply presents some of the tools the author uses in his everyday research.
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Fischer E (1894) Einfluss der configuration auf die wirkung der enzyme. Ber Dt Chem Ges 27:2985–2993
Dunker AK, Obradovic Z, Romero P, Garner EC, Brown CJ (2000) Intrinsic protein disorder in complete genomes. Genome Inform Ser Workshop Genome Inform 11:161–171
Uversky VN (2010) The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome. J Biomed Biotechnol 2010:568068
Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337(3):635–645
Dunker AK, Lawson JD, Brown CJ, Williams RM, Romero P, Oh JS, Oldfield CJ, Campen AM, Ratliff CM, Hipps KW, Ausio J, Nissen MS, Reeves R, Kang C, Kissinger CR, Bailey RW, Griswold MD, Chiu W, Garner EC, Obradovic Z (2001) Intrinsically disordered protein. J Mol Graph Model 19(1):26–59
Uversky VN, Dunker AK (2010) Understanding protein non-folding. Biochim Biophys Acta 1804(6):1231–1264
Xue B, Dunker AK, Uversky VN (2012) Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 30(2):137–149
Peng Z, Yan J, Fan X, Mizianty MJ, Xue B, Wang K, Hu G, Uversky VN, Kurgan L (2015) Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life. Cell Mol Life Sci 72(1):137–151
Obradovic Z, Peng K, Vucetic S, Radivojac P, Brown CJ, Dunker AK (2003) Predicting intrinsic disorder from amino acid sequence. Proteins 53(S6):566–572
Dunker AK, Garner E, Guilliot S, Romero P, Albrecht K, Hart J, Obradovic Z, Kissinger C, Villafranca JE (1998) Protein disorder and the evolution of molecular recognition: theory, predictions and observations. Pac Symp Biocomput 473–484
Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293(2):321–331
Uversky VN, Gillespie JR, Fink AL (2000) Why are “natively unfolded” proteins unstructured under physiologic conditions? Proteins 41(3):415–427
Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27(10):527–533
Daughdrill GW, Pielak GJ, Uversky VN, Cortese MS, Dunker AK (2005) Natively disordered proteins. In: Buchner J, Kiefhaber T (eds) Handbook of protein folding. Wiley-VCH, Verlag GmbH & Co., KGaA, Weinheim, Germany, pp 271–353
Uversky VN, Dunker AK (2013) The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biol Rep 5:1
Uversky VN (2003) Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell Mol Life Sci 60(9):1852–1871
Zhang T, Faraggi E, Li Z, Zhou Y (2013) Intrinsically semi-disordered state and its role in induced folding and protein aggregation. Cell Biochem Biophys 67(3):1193–1205
Uversky VN (2013) Unusual biophysics of intrinsically disordered proteins. Biochim Biophys Acta 1834(5):932–951
Uversky VN (2013) A decade and a half of protein intrinsic disorder: biology still waits for physics. Protein Sci 22(6):693–724
Uversky VN (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11(4):739–756
Bracken C, Iakoucheva LM, Romero PR, Dunker AK (2004) Combining prediction, computation and experiment for the characterization of protein disorder. Curr Opin Struct Biol 14(5):570–576
Receveur-Brechot V, Bourhis JM, Uversky VN, Canard B, Longhi S (2006) Assessing protein disorder and induced folding. Proteins 62(1):24–45
Uversky VN, Dunker AK (2012) Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes. Anal Chem 84(5):2096–2104
Uversky VN (2015) Biophysical methods to investigate intrinsically disordered proteins: avoiding an “Elephant and Blind Men” situation. Adv Exp Med Biol 870:215–260
Ringe D, Petsko GA (1986) Study of protein dynamics by X-ray diffraction. Methods Enzymol 131:389–433
Dyson HJ, Wright PE (2002) Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv Protein Chem 62:311–340
Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104(8):3607–3622
Dyson HJ, Wright PE (2005) Elucidation of the protein folding landscape by NMR. Methods Enzymol 394:299–321
Fasman GD (1996) Circular dichroism and the conformational analysis of biomolecules. Plenem Press, New York
Adler AJ, Greenfield NJ, Fasman GD (1973) Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol 27:675–735
Provencher SW, Glockner J (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20(1):33–37
Woody RW (1995) Circular dichroism. Methods Enzymol 246:34–71
Smyth E, Syme CD, Blanch EW, Hecht L, Vasak M, Barron LD (2001) Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers 58(2):138–151
Uversky VN (1999) A multiparametric approach to studies of self-organization of globular proteins. Biochemistry (Mosc) 64(3):250–266
Glatter O, Kratky O (1982) Small angle X-ray scattering. Academic, London
Markus G (1965) Protein substrate conformation and proteolysis. Proc Natl Acad Sci U S A 54:253–258
Mikhalyi E (1978) Application of proteolytic enzymes to protein structure studies. CRC Press, Boca Raton
Hubbard SJ, Eisenmenger F, Thornton JM (1994) Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci 3:757–768
Fontana A, de Laureto PP, de Filippis V, Scaramella E, Zambonin M (1997) Probing the partly folded states of proteins by limited proteolysis. Fold Des 2:R17–R26
Fontana A, de Laureto PP, Spolaore B, Frare E, Picotti P, Zambonin M (2004) Probing protein structure by limited proteolysis. Acta Biochim Pol 51(2):299–321
Iakoucheva LM, Kimzey AL, Masselon CD, Smith RD, Dunker AK, Ackerman EJ (2001) Aberrant mobility phenomena of the DNA repair protein XPA. Protein Sci 10:1353–1362
Privalov PL (1979) Stability of proteins: small globular proteins. Adv Protein Chem 33:167–241
Ptitsyn O (1995) Molten globule and protein folding. Adv Protein Chem 47:83–229
Ptitsyn OB, Uversky VN (1994) The molten globule is a third thermodynamical state of protein molecules. FEBS Lett 341:15–18
Uversky VN, Ptitsyn OB (1996) All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Fold Des 1(2):117–122
Westhof E, Altschuh D, Moras D, Bloomer AC, Mondragon A, Klug A, Van Regenmortel MH (1984) Correlation between segmental mobility and the location of antigenic determinants in proteins. Nature 311(5982):123–126
Berzofsky JA (1985) Intrinsic and extrinsic factors in protein antigenic structure. Science 229(4717):932–940
Romero P, Obradovic Z, Li X, Garner EC, Brown CJ, Dunker AK (2001) Sequence complexity of disordered protein. Proteins 42:38–48
Wootton JC (1993) Statistic of local complexity in amino acid sequences and sequence databases. Comput Chem 17:149–163
Radivojac P, Obradovic Z, Smith DK, Zhu G, Vucetic S, Brown CJ, Lawson JD, Dunker AK (2004) Protein flexibility and intrinsic disorder. Protein Sci 13(1):71–80
Romero P, Obradovic Z, Kissinger CR, Villafranca JE, Dunker AK (1997) Identifying disordered regions in proteins from amino acid sequences. IEEE Int Conf Neural Netw 1:90–95
Lise S, Jones DT (2005) Sequence patterns associated with disordered regions in proteins. Proteins 58(1):144–150
Ferron F, Longhi S, Canard B, Karlin D (2006) A practical overview of protein disorder prediction methods. Proteins 65(1):1–14
Dosztanyi Z, Sandor M, Tompa P, Simon I (2007) Prediction of protein disorder at the domain level. Curr Protein Pept Sci 8(2):161–171
He B, Wang K, Liu Y, Xue B, Uversky VN, Dunker AK (2009) Predicting intrinsic disorder in proteins: an overview. Cell Res 19(8):929–949
Kurgan L, Disfani FM (2011) Structural protein descriptors in 1-dimension and their sequence-based predictions. Curr Protein Pept Sci 12(6):470–489
Cozzetto D, Jones DT (2013) The contribution of intrinsic disorder prediction to the elucidation of protein function. Curr Opin Struct Biol 23(3):467–472
Atkins JD, Boateng SY, Sorensen T, McGuffin LJ (2015) Disorder prediction methods, their applicability to different protein targets and their usefulness for guiding experimental studies. Int J Mol Sci 16(8):19040–19054
Varadi M, Vranken W, Guharoy M, Tompa P (2015) Computational approaches for inferring the functions of intrinsically disordered proteins. Front Mol Biosci 2:45
Garner E, Romero P, Dunker AK, Brown C, Obradovic Z (1999) Predicting binding regions within disordered proteins. Genome Inform 10:41–50
Oldfield CJ, Cheng Y, Cortese MS, Romero P, Uversky VN, Dunker AK (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44(37):12454–12470
Mohan A, Oldfield CJ, Radivojac P, Vacic V, Cortese MS, Dunker AK, Uversky VN (2006) Analysis of molecular recognition features (MoRFs). J Mol Biol 362(5):1043–1059
Cheng Y, Oldfield CJ, Meng J, Romero P, Uversky VN, Dunker AK (2007) Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry 46(47):13468–13477
Disfani FM, Hsu WL, Mizianty MJ, Oldfield CJ, Xue B, Dunker AK, Uversky VN, Kurgan L (2012) MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins. Bioinformatics 28(12):i75–i83
Puntervoll P, Linding R, Gemund C, Chabanis-Davidson S, Mattingsdal M, Cameron S, Martin DM, Ausiello G, Brannetti B, Costantini A, Ferre F, Maselli V, Via A, Cesareni G, Diella F, Superti-Furga G, Wyrwicz L, Ramu C, McGuigan C, Gudavalli R, Letunic I, Bork P, Rychlewski L, Kuster B, Helmer-Citterich M, Hunter WN, Aasland R, Gibson TJ (2003) ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins. Nucleic Acids Res 31(13):3625–3630
Dosztanyi Z, Meszaros B, Simon I (2009) ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 25(20):2745–2746
Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347(4):827–839
Peng Z, Wang C, Uversky VN, Kurgan L (2016) Prediction of disordered RNA, DNA, and protein binding regions using DisoRDPbind. In: Kloczkowski A, Zhou Y, Faraggi E, Yang Y (eds) Prediction of protein secondary structure and other one-dimensional structural properties, Methods in molecular biology. Springer, New York
Iakoucheva LM, Radivojac P, Brown CJ, O'Connor TR, Sikes JG, Obradovic Z, Dunker AK (2004) The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res 32(3):1037–1049
Pejaver V, Hsu WL, Xin F, Dunker AK, Uversky VN, Radivojac P (2014) The structural and functional signatures of proteins that undergo multiple events of post-translational modification. Protein Sci 23(8):1077–1093
Uversky VN, Radivojac P, Iakoucheva LM, Obradovic Z, Dunker AK (2007) Prediction of intrinsic disorder and its use in functional proteomics. Methods Mol Biol 408:69–92
Ritter LM, Arakawa T, Goldberg AF (2005) Predicted and measured disorder in peripherin/rds, a retinal tetraspanin. Protein Pept Lett 12(7):677–686
Kukhtina V, Kottwitz D, Strauss H, Heise B, Chebotareva N, Tsetlin V, Hucho F (2006) Intracellular domain of nicotinic acetylcholine receptor: the importance of being unfolded. J Neurochem 97(Suppl 1):63–67
Yiu CP, Beavil RL, Chan HY (2006) Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble. Biochem Biophys Res Commun 343(1):311–318
Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL (2007) Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death Differ 14(1):128–136
Nardini M, Svergun D, Konarev PV, Spano S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M (2006) The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci 15(5):1042–1050
Roy S, Schnell S, Radivojac P (2006) Unraveling the nature of the segmentation clock: intrinsic disorder of clock proteins and their interaction map. Comput Biol Chem 30(4):241–248
Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S (2006) Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. Protein Expr Purif 47(2):398–404
Iakoucheva LM, Brown CJ, Lawson JD, Obradovic Z, Dunker AK (2002) Intrinsic disorder in cell-signaling and cancer-associated proteins. J Mol Biol 323:573–584
Cheng Y, Le Gall T, Oldfield CJ, Dunker AK, Uversky VN (2006) Abundance of intrinsic disorder in proteins associated with cardiovascular disease. Biochemistry 45(35):10448–10460
Liu J, Perumal NB, Oldfield CJ, Su EW, Uversky VN, Dunker AK (2006) Intrinsic disorder in transcription factors. Biochemistry 45(22):6873–6888
Singh GP, Ganapathi M, Sandhu KS, Dash D (2006) Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes. Proteins 62(2):309–315
Hansen JC, Lu X, Ross ED, Woody RW (2006) Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem 281(4):1853–1856
Peng Z, Mizianty MJ, Xue B, Kurgan L, Uversky VN (2012) More than just tails: intrinsic disorder in histone proteins. Mol Biosyst 8(7):1886–1901
Peng Z, Oldfield CJ, Xue B, Mizianty MJ, Dunker AK, Kurgan L, Uversky VN (2014) A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome. Cell Mol Life Sci 71(8):1477–1504
Xue B, Mizianty MJ, Kurgan L, Uversky VN (2012) Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cell Mol Life Sci 69(8):1211–1259
Fan X, Xue B, Dolan PT, LaCount DJ, Kurgan L, Uversky VN (2014) The intrinsic disorder status of the human hepatitis C virus proteome. Mol Biosyst 10(6):1345–1363
Xue B, Blocquel D, Habchi J, Uversky AV, Kurgan L, Uversky VN, Longhi S (2014) Structural disorder in viral proteins. Chem Rev 114(13):6880–6911
Meng F, Badierah RA, Almehdar HA, Redwan EM, Kurgan L, Uversky VN (2015) Unstructural biology of the dengue virus proteins. FEBS J 282(17):3368–3394
Goh GK, Dunker AK, Uversky VN (2015) Detection of links between Ebola nucleocapsid and virulence using disorder analysis. Mol Biosyst 11(8):2337–2344
Goh GK, Dunker AK, Uversky VN (2015) Shell disorder, immune evasion and transmission behaviors among human and animal retroviruses. Mol Biosyst 11(8):2312–2323
Dolan PT, Roth AP, Xue B, Sun R, Dunker AK, Uversky VN, LaCount DJ (2015) Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions. Protein Sci 24(2):221–235
Haynes C, Iakoucheva LM (2006) Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Res 34(1):305–312
Bustos DM, Iglesias AA (2006) Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins. Proteins 63(1):35–42
Denning DP, Patel SS, Uversky V, Fink AL, Rexach M (2003) Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A 100(5):2450–2455
Boeckmann B, Bairoch A, Apweiler R, Blatter M-C, Estreicher A, Gasteiger E, Martin MJ, Michoud K, O’Donovan C, Phan I, Pilbout S, Schneider M (2003) The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003. Nucleic Acids Res 31:365–370
Vucetic S, Obradovic Z, Vacic V, Radivojac P, Peng K, Iakoucheva LM, Cortese MS, Lawson JD, Brown CJ, Sikes JG, Newton CD, Dunker AK (2005) DisProt: a database of protein disorder. Bioinformatics 21(1):137–140
Sickmeier M, Hamilton JA, LeGall T, Vacic V, Cortese MS, Tantos A, Szabo B, Tompa P, Chen J, Uversky VN, Obradovic Z, Dunker AK (2007) DisProt: the database of disordered proteins. Nucleic Acids Res 35(Database issue):D786–D793
Vacic V, Uversky VN, Dunker AK, Lonardi S (2007) Composition profiler: a tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics 8:211
Peng K, Vucetic S, Radivojac P, Brown CJ, Dunker AK, Obradovic Z (2005) Optimizing long intrinsic disorder predictors with protein evolutionary information. J Bioinform Comput Biol 3(1):35–60
Obradovic Z, Peng K, Vucetic S, Radivojac P, Dunker AK (2005) Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 61(Suppl 7):176–182
Peng K, Radivojac P, Vucetic S, Dunker AK, Obradovic Z (2006) Length-dependent prediction of protein intrinsic disorder. BMC Bioinformatics 7(1):208
Xue B, Dunbrack RL, Williams RW, Dunker AK, Uversky VN (2010) PONDR-FIT: a meta-predictor of intrinsically disordered amino acids. Biochim Biophys Acta 1804(4):996–1010
Oldfield CJ, Cheng Y, Cortese MS, Brown CJ, Uversky VN, Dunker AK (2005) Comparing and combining predictors of mostly disordered proteins. Biochemistry 44(6):1989–2000
Oates ME, Romero P, Ishida T, Ghalwash M, Mizianty MJ, Xue B, Dosztanyi Z, Uversky VN, Obradovic Z, Kurgan L, Dunker AK, Gough J (2013) D(2)P(2): database of disordered protein predictions. Nucleic Acids Res 41(Database issue):D508–D516
Di Domenico T, Walsh I, Martin AJ, Tosatto SC (2012) MobiDB: a comprehensive database of intrinsic protein disorder annotations. Bioinformatics 28(15):2080–2081
Potenza E, Domenico TD, Walsh I, Tosatto SC (2015) MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins. Nucleic Acids Res 43(Database issue):D315–D320
Szklarczyk D, Franceschini A, Kuhn M, Simonovic M, Roth A, Minguez P, Doerks T, Stark M, Muller J, Bork P, Jensen L.J, von Mering C (2011) The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored. Nucleic Acids Res, 2011;39:D561–568
Vucetic S, Brown CJ, Dunker AK, Obradovic Z (2003) Flavors of protein disorder. Proteins 52:573–584
Prilusky J, Felder CE, Zeev-Ben-Mordehai T, Rydberg EH, Man O, Beckmann JS, Silman I, Sussman JL (2005) FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21(16):3435–3438
Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21(16):3433–3434
Campen A, Williams RM, Brown CJ, Meng J, Uversky VN, Dunker AK (2008) TOP-IDP-scale: a new amino acid scale measuring propensity for intrinsic disorder. Protein Pept Lett 15(9):956–963
Huang F, Oldfield C, Meng J, Hsu WL, Xue B, Uversky VN, Romero P, Dunker AK (2012) Subclassifying disordered proteins by the CH-CDF plot method. Pac Symp Biocomput 128–139
Huang F, Oldfield CJ, Xue B, Hsu WL, Meng J, Liu X, Shen L, Romero P, Uversky VN, Dunker A (2014) Improving protein order-disorder classification using charge-hydropathy plots. BMC Bioinformatics 15(Suppl 17):S4
Peng K, Radivojac P, Vucetic S, Dunker AK, Obradovic Z (2006) Length-dependent prediction of protein intrinsic disorder. BMC Bioinformatics 7
Ishida T, Kinoshita K (2007) PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res 35(Web Server issue):W460–W464
Walsh I, Martin AJ, Di Domenico T, Tosatto SC (2012) ESpritz: accurate and fast prediction of protein disorder. Bioinformatics 28(4):503–509
Linding R, Jensen LJ, Diella F, Bork P, Gibson TJ, Russell RB (2003) Protein disorder prediction: implications for structural proteomics. Structure 11(11):1453–1459
Linding R, Russell RB, Neduva V, Gibson TJ (2003) GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 31(13):3701–3708
Yang ZR, Thomson R, McNeil P, Esnouf RM (2005) RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21(16):3369–3376
Dyson HJ, Wright PE (2002) Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12(1):54–60
Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6(3):197–208
Vacic V, Oldfield CJ, Mohan A, Radivojac P, Cortese MS, Uversky VN, Dunker AK (2007) Characterization of molecular recognition features, MoRFs, and their binding partners. J Proteome Res 6(6):2351–2366
Uversky VN (2013) Intrinsic disorder-based protein interactions and their modulators. Curr Pharm Des 19(23):4191–4213
Daily KM, Radivojac P, Dunker AK. Intrinsic disorder and protein modifications: building an SVM predictor for methylation. In: IEEE symposium on computational intelligence in bioinformatics and computational biology, CIBCB 2005, San Diego, CA, USA, November 2005, pp 475–481
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This work was supported in part by a grant from the Russian Science Foundation RSCF № 14-24-00131.
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Uversky, V.N. (2017). How to Predict Disorder in a Protein of Interest. In: Zhou, Y., Kloczkowski, A., Faraggi, E., Yang, Y. (eds) Prediction of Protein Secondary Structure. Methods in Molecular Biology, vol 1484. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6406-2_11
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