메뉴 건너뛰기




Volumn 14, Issue 5, 2004, Pages 570-576

Combining prediction, computation and experiment for the characterization of protein disorder

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; ALGORITHM; AMINO ACID SEQUENCE; ANALYTIC METHOD; GENOME; MASS SPECTROMETRY; MOLECULAR INTERACTION; MONTE CARLO METHOD; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PREDICTION; PRESSURE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN STRUCTURE; REVIEW; TEMPERATURE DEPENDENCE;

EID: 4744349987     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.08.003     Document Type: Review
Times cited : (110)

References (64)
  • 1
    • 1342290303 scopus 로고    scopus 로고
    • Unfolded proteins
    • Amsterdam: Academic Press;
    • Rose GD (Ed): Unfolded proteins. In Advances in Protein Chemistry, vol 62. Amsterdam: Academic Press; 2002.
    • (2002) Advances in Protein Chemistry , vol.62
    • Rose, G.D.1
  • 5
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • P.E. Wright, and H.J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm J Mol Biol 293 1999 321 331
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 7
    • 0034669882 scopus 로고    scopus 로고
    • Why are 'natively unfolded' proteins unstructured under physiologic conditions?
    • V. Uversky, J. Gillespie, and A. Fink Why are 'natively unfolded' proteins unstructured under physiologic conditions? Proteins 41 2000 415 427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.1    Gillespie, J.2    Fink, A.3
  • 9
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • Liu J, Rost B: NORSp: predictions of long regions without regular secondary structure. Nucleic Acids Res 2003; 31:3833-3835. [URL: http://cubic.bioc.columbia.edu/services/NORSp ].
    • (2003) Nucleic Acids Res , vol.31 , pp. 3833-3835
    • Liu, J.1    Rost, B.2
  • 10
    • 0242362157 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins from position specific score matrices
    • D.T. Jones, and J.J. Ward Prediction of disordered regions in proteins from position specific score matrices Proteins 53 suppl 6 2003 573 578
    • (2003) Proteins , vol.53 , Issue.6 , pp. 573-578
    • Jones, D.T.1    Ward, J.J.2
  • 12
    • 0242267501 scopus 로고    scopus 로고
    • Evaluation of disorder predictions in CASP5
    • E. Melamud, and J. Moult Evaluation of disorder predictions in CASP5 Proteins 53 suppl 6 2003 561 565
    • (2003) Proteins , vol.53 , Issue.6 , pp. 561-565
    • Melamud, E.1    Moult, J.2
  • 13
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • A. Bax Weak alignment offers new NMR opportunities to study protein structure and dynamics Protein Sci 12 2003 1 16 This is an excellent introductory review on dipolar coupling.
    • (2003) Protein Sci , vol.12 , pp. 1-16
    • Bax, A.1
  • 14
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • A.G. Palmer III, C.D. Kroenke, and J.P. Loria Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules Methods Enzymol 339 2001 204 238
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 15
    • 0035014892 scopus 로고    scopus 로고
    • NMR spin relaxation methods for characterization of disorder and folding in proteins
    • C. Bracken NMR spin relaxation methods for characterization of disorder and folding in proteins J Mol Graph Model 19 2001 3 12
    • (2001) J Mol Graph Model , vol.19 , pp. 3-12
    • Bracken, C.1
  • 16
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • H.J. Dyson, and P.E. Wright Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states Methods Enzymol 339 2001 258 270
    • (2001) Methods Enzymol , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 17
    • 0031064317 scopus 로고    scopus 로고
    • Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins
    • O. Zhang, J.D. Forman-Kay, D. Shortle, and L.E. Kay Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins J Biomol NMR 9 1997 181 200
    • (1997) J Biomol NMR , vol.9 , pp. 181-200
    • Zhang, O.1    Forman-Kay, J.D.2    Shortle, D.3    Kay, L.E.4
  • 18
    • 0242362190 scopus 로고    scopus 로고
    • Many residues in cytochrome c populate alternative states under equilibrium conditions
    • M.P. Williamson Many residues in cytochrome c populate alternative states under equilibrium conditions Proteins 53 2003 731 739
    • (2003) Proteins , vol.53 , pp. 731-739
    • Williamson, M.P.1
  • 19
    • 1542533572 scopus 로고    scopus 로고
    • Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: The villin headpiece subdomain
    • Y. Tang, D.J. Rigotti, R. Fairman, and D.P. Raleigh Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain Biochemistry 43 2004 3264 3272
    • (2004) Biochemistry , vol.43 , pp. 3264-3272
    • Tang, Y.1    Rigotti, D.J.2    Fairman, R.3    Raleigh, D.P.4
  • 22
    • 0037442335 scopus 로고    scopus 로고
    • Side chain dynamics in unfolded protein states: An NMR based 2H spin relaxation study of delta131delta
    • 2D methyl groups specific for unfolded proteins. A correlation between backbone and sidechain dynamics is observed. Motional differences between methyl groups suggest the presence of hydrophobic clustering.
    • (2003) J Am Chem Soc , vol.125 , pp. 1748-1758
    • Choy, W.Y.1    Shortle, D.2    Kay, L.E.3
  • 23
    • 0141843568 scopus 로고    scopus 로고
    • Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: An application to delta131delta
    • W.Y. Choy, and L.E. Kay Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta J Am Chem Soc 125 2003 11988 11992
    • (2003) J Am Chem Soc , vol.125 , pp. 11988-11992
    • Choy, W.Y.1    Kay, L.E.2
  • 24
    • 0037159208 scopus 로고    scopus 로고
    • Molecular hinges in protein folding: The urea-denatured state of apomyoglobin
    • S. Schwarzinger, P.E. Wright, and H.J. Dyson Molecular hinges in protein folding: the urea-denatured state of apomyoglobin Biochemistry 41 2002 12681 12686
    • (2002) Biochemistry , vol.41 , pp. 12681-12686
    • Schwarzinger, S.1    Wright, P.E.2    Dyson, H.J.3
  • 25
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • D. Shortle, and M.S. Ackerman Persistence of native-like topology in a denatured protein in 8 M urea Science 293 2001 487 489
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 26
    • 1842426942 scopus 로고    scopus 로고
    • Direct demonstration of structural similarity between native and denatured eglin C
    • S. Ohnishi, A.L. Lee, M.H. Edgell, and D. Shortle Direct demonstration of structural similarity between native and denatured eglin C Biochemistry 43 2004 4064 4070
    • (2004) Biochemistry , vol.43 , pp. 4064-4070
    • Ohnishi, S.1    Lee, A.L.2    Edgell, M.H.3    Shortle, D.4
  • 29
    • 0037157124 scopus 로고    scopus 로고
    • Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy
    • M. Tollinger, J.D. Forman-Kay, and L.E. Kay Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy J Am Chem Soc 124 2002 5714 5717
    • (2002) J Am Chem Soc , vol.124 , pp. 5714-5717
    • Tollinger, M.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 30
    • 0037120882 scopus 로고    scopus 로고
    • Solution NMR techniques for large molecular and supramolecular structures
    • R. Riek, J. Fiaux, E.B. Bertelsen, A.L. Horwich, and K. Wuthrich Solution NMR techniques for large molecular and supramolecular structures J Am Chem Soc 124 2002 12144 12153
    • (2002) J Am Chem Soc , vol.124 , pp. 12144-12153
    • Riek, R.1    Fiaux, J.2    Bertelsen, E.B.3    Horwich, A.L.4    Wuthrich, K.5
  • 32
    • 0037007467 scopus 로고    scopus 로고
    • 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa
    • M.R. Arnold, W. Kremer, H.D. Ludemann, and H.R. Kalbitzer 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa Biophys Chem 96 2002 129 140
    • (2002) Biophys Chem , vol.96 , pp. 129-140
    • Arnold, M.R.1    Kremer, W.2    Ludemann, H.D.3    Kalbitzer, H.R.4
  • 33
    • 1642488929 scopus 로고    scopus 로고
    • Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
    • T.N. Niraula, T. Konno, H. Li, H. Yamada, K. Akasaka, and H. Tachibana Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils Proc Natl Acad Sci USA 101 2004 4089 4093
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4089-4093
    • Niraula, T.N.1    Konno, T.2    Li, H.3    Yamada, H.4    Akasaka, K.5    Tachibana, H.6
  • 34
    • 4744351381 scopus 로고    scopus 로고
    • Slow conformational dynamics in the hamster prion protein
    • K. Kuwata, Y.O. Kamatari, K. Akasaka, and T.L. James Slow conformational dynamics in the hamster prion protein Biochemistry 43 2004 4439 4446
    • (2004) Biochemistry , vol.43 , pp. 4439-4446
    • Kuwata, K.1    Kamatari, Y.O.2    Akasaka, K.3    James, T.L.4
  • 35
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • A.G. Palmer III NMR probes of molecular dynamics: overview and comparison with other techniques Annu Rev Biophys Biomol Struct 30 2001 129 155
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 36
    • 0037668073 scopus 로고    scopus 로고
    • Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution
    • L. Vugmeyster, D.P. Raleigh, A.G. Palmer III, and B.E. Vugmeister Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution J Am Chem Soc 125 2003 8400 8404 This work provides better estimation of the accuracy of the motional parameters and the influence of correlated motions on the interpretation of NMR relaxation analysis.
    • (2003) J Am Chem Soc , vol.125 , pp. 8400-8404
    • Vugmeyster, L.1    Raleigh, D.P.2    Palmer III, A.G.3    Vugmeister, B.E.4
  • 37
    • 0034885557 scopus 로고    scopus 로고
    • Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies
    • A.V. Buevich, U.P. Shinde, M. Inouye, and J. Baum Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies J Biomol NMR 20 2001 233 249
    • (2001) J Biomol NMR , vol.20 , pp. 233-249
    • Buevich, A.V.1    Shinde, U.P.2    Inouye, M.3    Baum, J.4
  • 38
    • 0347914553 scopus 로고    scopus 로고
    • Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR
    • K. Ding, J.M. Louis, and A.M. Gronenborn Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR J Mol Biol 335 2004 1299 1307
    • (2004) J Mol Biol , vol.335 , pp. 1299-1307
    • Ding, K.1    Louis, J.M.2    Gronenborn, A.M.3
  • 39
    • 0346219438 scopus 로고    scopus 로고
    • On the origin of residual dipolar couplings from denatured proteins
    • M. Louhivuori, K. Paakkonen, K. Fredriksson, P. Permi, J. Lounila, and A. Annila On the origin of residual dipolar couplings from denatured proteins J Am Chem Soc 125 2003 15647 15650 The authors' calculation and simulations demonstrate that RDC values for a random-coil polymer are non-zero. Steric interactions within the amino acid sequence introduce local orientation within the random flight polymer chain. The net effect is that RDC at the termini will tend toward zero, whereas internal sequences will have non-vanishing values.
    • (2003) J Am Chem Soc , vol.125 , pp. 15647-15650
    • Louhivuori, M.1    Paakkonen, K.2    Fredriksson, K.3    Permi, P.4    Lounila, J.5    Annila, A.6
  • 40
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • N.K. Goto, and L.E. Kay New developments in isotope labeling strategies for protein solution NMR spectroscopy Curr Opin Struct Biol 10 2000 585 592
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 41
    • 0041846681 scopus 로고    scopus 로고
    • Aromatic and methyl NOEs highlight hydrophobic clustering in the unfolded state of an SH3 domain
    • K.A. Crowhurst, and J.D. Forman-Kay Aromatic and methyl NOEs highlight hydrophobic clustering in the unfolded state of an SH3 domain Biochemistry 42 2003 8687 8695
    • (2003) Biochemistry , vol.42 , pp. 8687-8695
    • Crowhurst, K.A.1    Forman-Kay, J.D.2
  • 42
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • J.R. Gillespie, and D. Shortle Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels J Mol Biol 268 1997 158 169
    • (1997) J Mol Biol , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 43
    • 0036438881 scopus 로고    scopus 로고
    • Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling
    • K. Teilum, B.B. Kragelund, and F.M. Poulsen Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling J Mol Biol 324 2002 349 357
    • (2002) J Mol Biol , vol.324 , pp. 349-357
    • Teilum, K.1    Kragelund, B.B.2    Poulsen, F.M.3
  • 44
    • 0036389787 scopus 로고    scopus 로고
    • Mapping long-range contacts in a highly unfolded protein
    • M.A. Lietzow, M. Jamin, H.J. Jane Dyson, and P.E. Wright Mapping long-range contacts in a highly unfolded protein J Mol Biol 322 2002 655 662
    • (2002) J Mol Biol , vol.322 , pp. 655-662
    • Lietzow, M.A.1    Jamin, M.2    Jane Dyson, H.J.3    Wright, P.E.4
  • 45
    • 1642535628 scopus 로고    scopus 로고
    • EX1 hydrogen exchange and protein folding
    • D.M. Ferraro, and A.D. Robertson EX1 hydrogen exchange and protein folding Biochemistry 43 2004 587 594 This review describes the application of slow amide hydrogen exchange to study the kinetics of protein folding and unfolding. The advantages of EX1-type hydrogen exchange over traditional folding experiments are emphasized.
    • (2004) Biochemistry , vol.43 , pp. 587-594
    • Ferraro, D.M.1    Robertson, A.D.2
  • 46
    • 1842868694 scopus 로고    scopus 로고
    • Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes
    • X. Yan, J. Watson, P.S. Ho, and M.L. Deinzer Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes Mol Cell Proteomics 3 2004 10 23
    • (2004) Mol Cell Proteomics , vol.3 , pp. 10-23
    • Yan, X.1    Watson, J.2    Ho, P.S.3    Deinzer, M.L.4
  • 47
    • 1842861593 scopus 로고    scopus 로고
    • High-sensitivity mass spectrometry for imaging subunit interactions: Hydrogen/deuterium exchange
    • J. Lanman, and P.E. Prevelige High-sensitivity mass spectrometry for imaging subunit interactions: hydrogen/deuterium exchange Curr Opin Struct Biol 14 2004 181 188
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 181-188
    • Lanman, J.1    Prevelige, P.E.2
  • 48
    • 1642463331 scopus 로고    scopus 로고
    • Mass spectrometry on segment-specific hydrogen exchange of dihydrofolate reductase
    • T. Yamamoto, S. Izumi, and K. Gekko Mass spectrometry on segment-specific hydrogen exchange of dihydrofolate reductase J Biochem (Tokyo) 135 2004 17 24
    • (2004) J Biochem (Tokyo) , vol.135 , pp. 17-24
    • Yamamoto, T.1    Izumi, S.2    Gekko, K.3
  • 50
    • 0242386421 scopus 로고    scopus 로고
    • Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins
    • L. Cravello, D. Lascoux, and E. Forest Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins Rapid Commun Mass Spectrom 17 2003 2387 2393
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 2387-2393
    • Cravello, L.1    Lascoux, D.2    Forest, E.3
  • 51
    • 1842857772 scopus 로고    scopus 로고
    • Rapid analysis of protein structure and dynamics by hydrogen/deuterium exchange mass spectrometry
    • Y. Hamuro, S.J. Coales, M.R. Southern, J.F. Nemeth-Cawley, D.D. Stranz, and P.R. Griffin Rapid analysis of protein structure and dynamics by hydrogen/deuterium exchange mass spectrometry J Biomol Tech 14 2003 171 182 An excellent review describing recent advances in protein structure and dynamics characterization using HXMS.
    • (2003) J Biomol Tech , vol.14 , pp. 171-182
    • Hamuro, Y.1    Coales, S.J.2    Southern, M.R.3    Nemeth-Cawley, J.F.4    Stranz, D.D.5    Griffin, P.R.6
  • 52
    • 1642514905 scopus 로고    scopus 로고
    • Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS
    • D. Pantazatos, J.S. Kim, H.E. Klock, R.C. Stevens, I.A. Wilson, S.A. Lesley, and V.L. Woods Jr. Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS Proc Natl Acad Sci USA 101 2004 751 756 This paper describes the application of amide hydrogen high-throughput and high-resolution deuterium exchange MS for rapid identification of disordered protein regions. Examples showing the improved crystallization of poorly crystallizing/diffracting proteins after the removal of such regions are also given.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 751-756
    • Pantazatos, D.1    Kim, J.S.2    Klock, H.E.3    Stevens, R.C.4    Wilson, I.A.5    Lesley, S.A.6    Woods Jr., V.L.7
  • 53
    • 0345598912 scopus 로고    scopus 로고
    • Structures and relative free energies of partially folded states of proteins
    • M. Vendruscolo, E. Paci, M. Karplus, and C.M. Dobson Structures and relative free energies of partially folded states of proteins Proc Natl Acad Sci USA 100 2003 14817 14821
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14817-14821
    • Vendruscolo, M.1    Paci, E.2    Karplus, M.3    Dobson, C.M.4
  • 54
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • W.Y. Choy, and J.D. Forman-Kay Calculation of ensembles of structures representing the unfolded state of an SH3 domain J Mol Biol 308 2001 1011 1032
    • (2001) J Mol Biol , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 55
    • 0037627721 scopus 로고    scopus 로고
    • Simulating disorder-order transitions in molecular recognition of unstructured proteins: Where folding meets binding
    • G.M. Verkhivker, D. Bouzida, D.K. Gehlhaar, P.A. Rejto, S.T. Freer, and P.W. Rose Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding Proc Natl Acad Sci USA 100 2003 5148 5153
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5148-5153
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5    Rose, P.W.6
  • 56
    • 0036084260 scopus 로고    scopus 로고
    • Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins
    • C.J. Tsai, P. Polverino de Laureto, A. Fontana, and R. Nussinov Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins Protein Sci 11 2002 1753 1770
    • (2002) Protein Sci , vol.11 , pp. 1753-1770
    • Tsai, C.J.1    Polverino De Laureto, P.2    Fontana, A.3    Nussinov, R.4
  • 57
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • 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 J Mol Biol 337 2004 635 645 The greater occurrence of disorder in eukaryotes, compared to prokaryotes and archaea, and the frequent use of disorder in signaling and regulation are further supported in this paper. A novel and interesting feature of this work is the use of gene ontology (GO) terms to estimate the over- and under-representation of predicted disorder in the molecular function, biological process and cellular component ontologies. DISOPRED2 is available at http://bioinf.cs.ucl.ac.uk/disopred/.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 58
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ: GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res 2003, 31:3701-3708. [URL: http://globplot.embl.de/. ]
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 59
    • 0036968309 scopus 로고    scopus 로고
    • Loopy proteins appear conserved in evolution
    • J. Liu, H. Tan, and B. Rost Loopy proteins appear conserved in evolution J Mol Biol 322 2002 53 64
    • (2002) J Mol Biol , vol.322 , pp. 53-64
    • Liu, J.1    Tan, H.2    Rost, B.3
  • 60
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • S. Longhi, V. Receveur-Brechot, D. Karlin, K. Johansson, H. Darbon, D. Bhella, R. Yeo, S. Finet, and B. Canard The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein J Biol Chem 278 2003 18638 18648 This paper demonstrates the potential advantage of using prediction to guide experimental analysis of proteins with both ordered and disordered regions.
    • (2003) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5    Bhella, D.6    Yeo, R.7    Finet, S.8    Canard, B.9
  • 62
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • J.M. Bourhis, K. Johansson, V. Receveur-Brechot, C.J. Oldfield, K.A. Dunker, B. Canard, and S. Longhi The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner Virus Res 99 2004 157 167
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5    Canard, B.6    Longhi, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.