메뉴 건너뛰기




Volumn 589, Issue 19, 2015, Pages 2570-2577

A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins

Author keywords

Disorder; Flexibility; Intrinsically disordered protein; Small angle scattering; Small angle X ray scattering

Indexed keywords

INTRINSICALLY DISORDERED PROTEIN;

EID: 84942297359     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.08.027     Document Type: Review
Times cited : (481)

References (95)
  • 1
    • 4344716256 scopus 로고    scopus 로고
    • Random-coil behavior and the dimensions of chemically unfolded proteins
    • J.E. Kohn, and et al. Random-coil behavior and the dimensions of chemically unfolded proteins Proc. Natl. Acad. Sci. U.S.A. 101 2004 12491 12496
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12491-12496
    • Kohn, J.E.1
  • 2
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • D.K. Wilkins, S.B. Grimshaw, V. Receveur, C.M. Dobson, J.A. Jones, and L.J. Smith Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques Biochemistry 38 1999 16424 16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 3
    • 37549043949 scopus 로고    scopus 로고
    • Interaction of urea with amino acids: Implications for urea-induced protein denaturation
    • M.C. Stumpe, and H. Grubmuller Interaction of urea with amino acids: implications for urea-induced protein denaturation J. Am. Chem. Soc. 129 2007 16126 16131
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 16126-16131
    • Stumpe, M.C.1    Grubmuller, H.2
  • 4
    • 77649338894 scopus 로고    scopus 로고
    • Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea
    • L. Galantini, C. Leggio, P.V. Konarev, and N.V. Pavel Human serum albumin binding ibuprofen: a 3D description of the unfolding pathway in urea Biophys. Chem. 147 2010 111 122
    • (2010) Biophys. Chem. , vol.147 , pp. 111-122
    • Galantini, L.1    Leggio, C.2    Konarev, P.V.3    Pavel, N.V.4
  • 6
    • 77956187980 scopus 로고    scopus 로고
    • Time-resolved X-ray scattering and RNA folding
    • L. Pollack, and S. Doniach Time-resolved X-ray scattering and RNA folding Methods Enzymol. 469 2009 253 268
    • (2009) Methods Enzymol. , vol.469 , pp. 253-268
    • Pollack, L.1    Doniach, S.2
  • 7
    • 51949084084 scopus 로고    scopus 로고
    • Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33
    • A.R. Round, and et al. Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33 J. Appl. Crystallogr. 41 2008 913 917
    • (2008) J. Appl. Crystallogr. , vol.41 , pp. 913-917
    • Round, A.R.1
  • 8
    • 68349097394 scopus 로고    scopus 로고
    • Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
    • G.L. Hura, and et al. Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS) Nat. Methods 6 2009 606 612
    • (2009) Nat. Methods , vol.6 , pp. 606-612
    • Hura, G.L.1
  • 9
    • 0035933335 scopus 로고    scopus 로고
    • Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
    • M. Aslam, and S.J. Perkins Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling J. Mol. Biol. 309 2001 1117 1138
    • (2001) J. Mol. Biol. , vol.309 , pp. 1117-1138
    • Aslam, M.1    Perkins, S.J.2
  • 10
    • 24944542708 scopus 로고    scopus 로고
    • Statistical coil model of the unfolded state: Resolving the reconciliation problem
    • A.K. Jha, A. Colubri, K.F. Freed, and T.R. Sosnick Statistical coil model of the unfolded state: resolving the reconciliation problem Proc. Natl. Acad. Sci. U.S.A. 102 2005 13099 13104
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13099-13104
    • Jha, A.K.1    Colubri, A.2    Freed, K.F.3    Sosnick, T.R.4
  • 11
    • 79959240249 scopus 로고    scopus 로고
    • Binary classification of protein molecules into intrinsically disordered and ordered segments
    • S. Fukuchi, K. Hosoda, K. Homma, T. Gojobori, and K. Nishikawa Binary classification of protein molecules into intrinsically disordered and ordered segments BMC Struct. Biol. 11 2011 29
    • (2011) BMC Struct. Biol. , vol.11 , pp. 29
    • Fukuchi, S.1    Hosoda, K.2    Homma, K.3    Gojobori, T.4    Nishikawa, K.5
  • 13
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 14
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • V.N. Uversky, C.J. Oldfield, and A.K. Dunker Intrinsically disordered proteins in human diseases: introducing the D2 concept Annu. Rev. Biophys. 37 2008 215 246
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 15
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 16
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 17
    • 79958044914 scopus 로고    scopus 로고
    • Unstructural biology coming of age
    • P. Tompa Unstructural biology coming of age Curr. Opin. Struct. Biol. 21 2011 419 425
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 419-425
    • Tompa, P.1
  • 19
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • P. Tompa, and M. Fuxreiter Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions Trends Biochem. Sci. 33 2008 2 8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 20
    • 79958712678 scopus 로고    scopus 로고
    • Biophysical analysis and small-angle X-ray scattering-derived structures of MeCP2-nucleosome complexes
    • C. Yang, M.J. van der Woerd, U.M. Muthurajan, J.C. Hansen, and K. Luger Biophysical analysis and small-angle X-ray scattering-derived structures of MeCP2-nucleosome complexes Nucleic Acids Res. 39 2011 4122 4135
    • (2011) Nucleic Acids Res. , vol.39 , pp. 4122-4135
    • Yang, C.1    Van Der Woerd, M.J.2    Muthurajan, U.M.3    Hansen, J.C.4    Luger, K.5
  • 21
    • 34248579736 scopus 로고    scopus 로고
    • The N terminus of Saccharomyces cerevisiae Msh6 is an unstructured tether to PCNA
    • S.S. Shell, C.D. Putnam, and R.D. Kolodner The N terminus of Saccharomyces cerevisiae Msh6 is an unstructured tether to PCNA Mol. Cell 26 2007 565 578
    • (2007) Mol. Cell , vol.26 , pp. 565-578
    • Shell, S.S.1    Putnam, C.D.2    Kolodner, R.D.3
  • 22
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • H.D. Mertens, and D.I. Svergun Structural characterization of proteins and complexes using small-angle X-ray solution scattering J. Struct. Biol. 172 2010 128 141
    • (2010) J. Struct. Biol. , vol.172 , pp. 128-141
    • Mertens, H.D.1    Svergun, D.I.2
  • 23
    • 77950223101 scopus 로고    scopus 로고
    • Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls
    • D.A. Jacques, and J. Trewhella Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls Protein Sci. 19 2010 642 657
    • (2010) Protein Sci. , vol.19 , pp. 642-657
    • Jacques, D.A.1    Trewhella, J.2
  • 25
    • 84924228248 scopus 로고    scopus 로고
    • Limiting radiation damage for high-brilliance biological solution scattering: Practical experience at the EMBL P12 beamline PETRAIII
    • C.M. Jeffries, M.A. Graewert, D.I. Svergun, and C.E. Blanchet Limiting radiation damage for high-brilliance biological solution scattering: practical experience at the EMBL P12 beamline PETRAIII J. Synchrotron Radiat. 22 2015 273 279
    • (2015) J. Synchrotron Radiat. , vol.22 , pp. 273-279
    • Jeffries, C.M.1    Graewert, M.A.2    Svergun, D.I.3    Blanchet, C.E.4
  • 28
    • 0002622807 scopus 로고
    • Data evaluation in small-angle scattering - Calculation of radial electron-density distribution by means of indirect fourier transformation
    • O. Glatter Data evaluation in small-angle scattering - calculation of radial electron-density distribution by means of indirect fourier transformation Acta Phys. Aust. 47 1977 83 102
    • (1977) Acta Phys. Aust. , vol.47 , pp. 83-102
    • Glatter, O.1
  • 29
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 30
    • 0034966446 scopus 로고    scopus 로고
    • Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering
    • J. Perez, P. Vachette, D. Russo, M. Desmadril, and D. Durand Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering J. Mol. Biol. 308 2001 721 743
    • (2001) J. Mol. Biol. , vol.308 , pp. 721-743
    • Perez, J.1    Vachette, P.2    Russo, D.3    Desmadril, M.4    Durand, D.5
  • 31
    • 72049093998 scopus 로고    scopus 로고
    • A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering
    • P. Bernado, and M. Blackledge A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering Biophys. J. 97 2009 2839 2845
    • (2009) Biophys. J. , vol.97 , pp. 2839-2845
    • Bernado, P.1    Blackledge, M.2
  • 33
    • 82655179899 scopus 로고    scopus 로고
    • Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering
    • P. Bernado, and D.I. Svergun Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering Mol. Biosyst. 8 2012 151 167
    • (2012) Mol. Biosyst. , vol.8 , pp. 151-167
    • Bernado, P.1    Svergun, D.I.2
  • 35
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 37
    • 69849103777 scopus 로고    scopus 로고
    • Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
    • M.R. Jensen, P.R. Markwick, S. Meier, C. Griesinger, M. Zweckstetter, S. Grzesiek, P. Bernado, and M. Blackledge Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings Structure 17 2009 1169 1185
    • (2009) Structure , vol.17 , pp. 1169-1185
    • Jensen, M.R.1    Markwick, P.R.2    Meier, S.3    Griesinger, C.4    Zweckstetter, M.5    Grzesiek, S.6    Bernado, P.7    Blackledge, M.8
  • 38
    • 44449116120 scopus 로고    scopus 로고
    • Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
    • M. Wells, and et al. Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain Proc. Natl. Acad. Sci. U.S.A. 105 2008 5762 5767
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5762-5767
    • Wells, M.1
  • 39
    • 1442300995 scopus 로고    scopus 로고
    • Polymer models of protein stability, folding, and interactions
    • H.X. Zhou Polymer models of protein stability, folding, and interactions Biochemistry 43 2004 2141 2154
    • (2004) Biochemistry , vol.43 , pp. 2141-2154
    • Zhou, H.X.1
  • 40
    • 78650811435 scopus 로고    scopus 로고
    • Structural biology: Proteins in dynamic equilibrium
    • P. Bernado, and M. Blackledge Structural biology: proteins in dynamic equilibrium Nature 468 2010 1046 1048
    • (2010) Nature , vol.468 , pp. 1046-1048
    • Bernado, P.1    Blackledge, M.2
  • 41
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • P. Bernado, E. Mylonas, M.V. Petoukhov, M. Blackledge, and D.I. Svergun Structural characterization of flexible proteins using small-angle X-ray scattering J. Am. Chem. Soc. 129 2007 5656 5664
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 42
    • 84936847118 scopus 로고    scopus 로고
    • Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering
    • G. Tria, H.D.T. Mertens, M. Kachala, and D.I. Svergun Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering Iucrj 2 2015 207 217
    • (2015) Iucrj , vol.2 , pp. 207-217
    • Tria, G.1    Mertens, H.D.T.2    Kachala, M.3    Svergun, D.I.4
  • 43
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • M. Pelikan, G.L. Hura, and M. Hammel Structure and flexibility within proteins as identified through small angle X-ray scattering Gen. Physiol. Biophys. 28 2009 174 189
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 45
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • B. Rozycki, Y.C. Kim, and G. Hummer SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions Structure 19 2011 109 116
    • (2011) Structure , vol.19 , pp. 109-116
    • Rozycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 46
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D.I. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 47
    • 84901036159 scopus 로고    scopus 로고
    • The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold
    • T. Schulte, and et al. The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold Open Biol. 4 2014 130090
    • (2014) Open Biol. , vol.4 , pp. 130090
    • Schulte, T.1
  • 49
    • 84884805102 scopus 로고    scopus 로고
    • Small angle X-ray scattering studies of mitochondrial glutaminase C reveal extended flexible regions, and link oligomeric state with enzyme activity
    • M. Moller, and et al. Small angle X-ray scattering studies of mitochondrial glutaminase C reveal extended flexible regions, and link oligomeric state with enzyme activity PLoS One 8 2013 e74783
    • (2013) PLoS One , vol.8 , pp. e74783
    • Moller, M.1
  • 50
    • 0036366575 scopus 로고    scopus 로고
    • Detecting native protein folds among large decoy sets with hydrophobic moment profiling
    • R. Zhou, and B.D. Silverman Detecting native protein folds among large decoy sets with hydrophobic moment profiling Pac. Symp. Biocomput. 2002 673 684
    • (2002) Pac. Symp. Biocomput. , pp. 673-684
    • Zhou, R.1    Silverman, B.D.2
  • 51
    • 0037424614 scopus 로고    scopus 로고
    • Computational simulation of the statistical properties of unfolded proteins
    • D.P. Goldenberg Computational simulation of the statistical properties of unfolded proteins J. Mol. Biol. 326 2003 1615 1633
    • (2003) J. Mol. Biol. , vol.326 , pp. 1615-1633
    • Goldenberg, D.P.1
  • 52
    • 4344704080 scopus 로고    scopus 로고
    • Reassessing random-coil statistics in unfolded proteins
    • N.C. Fitzkee, and G.D. Rose Reassessing random-coil statistics in unfolded proteins Proc. Natl. Acad. Sci. U.S.A. 101 2004 12497 12502
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12497-12502
    • Fitzkee, N.C.1    Rose, G.D.2
  • 53
    • 23944453852 scopus 로고    scopus 로고
    • Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteins
    • H.T. Tran, X. Wang, and R.V. Pappu Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteins Biochemistry 44 2005 11369 11380
    • (2005) Biochemistry , vol.44 , pp. 11369-11380
    • Tran, H.T.1    Wang, X.2    Pappu, R.V.3
  • 54
    • 21744448828 scopus 로고    scopus 로고
    • Scaling behavior and structure of denatured proteins
    • F. Ding, R.K. Jha, and N.V. Dokholyan Scaling behavior and structure of denatured proteins Structure 13 2005 1047 1054
    • (2005) Structure , vol.13 , pp. 1047-1054
    • Ding, F.1    Jha, R.K.2    Dokholyan, N.V.3
  • 55
    • 34447578997 scopus 로고    scopus 로고
    • Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins
    • Z. Wang, K.W. Plaxco, and D.E. Makarov Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins Biopolymers 86 2007 321 328
    • (2007) Biopolymers , vol.86 , pp. 321-328
    • Wang, Z.1    Plaxco, K.W.2    Makarov, D.E.3
  • 56
    • 40849106253 scopus 로고    scopus 로고
    • Small-angle X-ray scattering of reduced ribonuclease A: Effects of solution conditions and comparisons with a computational model of unfolded proteins
    • Y. Wang, J. Trewhella, and D.P. Goldenberg Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins J. Mol. Biol. 377 2008 1576 1592
    • (2008) J. Mol. Biol. , vol.377 , pp. 1576-1592
    • Wang, Y.1    Trewhella, J.2    Goldenberg, D.P.3
  • 58
    • 77950418698 scopus 로고    scopus 로고
    • Structural dynamics and single-stranded DNA binding activity of the three N-terminal domains of the large subunit of replication protein A from small angle X-ray scattering
    • D.I. Pretto, S. Tsutakawa, C.A. Brosey, A. Castillo, M.E. Chagot, J.A. Smith, J.A. Tainer, and W.J. Chazin Structural dynamics and single-stranded DNA binding activity of the three N-terminal domains of the large subunit of replication protein A from small angle X-ray scattering Biochemistry 49 2010 2880 2889
    • (2010) Biochemistry , vol.49 , pp. 2880-2889
    • Pretto, D.I.1    Tsutakawa, S.2    Brosey, C.A.3    Castillo, A.4    Chagot, M.E.5    Smith, J.A.6    Tainer, J.A.7    Chazin, W.J.8
  • 59
    • 0030699525 scopus 로고    scopus 로고
    • A circular dichroism study of preferential hydration and alcohol effects on a denatured protein, pig calpastatin domain i
    • T. Konno, N. Tanaka, M. Kataoka, E. Takano, and M. Maki A circular dichroism study of preferential hydration and alcohol effects on a denatured protein, pig calpastatin domain I Biochim. Biophys. Acta 1342 1997 73 82
    • (1997) Biochim. Biophys. Acta , vol.1342 , pp. 73-82
    • Konno, T.1    Tanaka, N.2    Kataoka, M.3    Takano, E.4    Maki, M.5
  • 60
    • 4444311182 scopus 로고    scopus 로고
    • Conformational prerequisites for formation of amyloid fibrils from histones
    • L.A. Munishkina, A.L. Fink, and V.N. Uversky Conformational prerequisites for formation of amyloid fibrils from histones J. Mol. Biol. 342 2004 1305 1324
    • (2004) J. Mol. Biol. , vol.342 , pp. 1305-1324
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 61
  • 62
    • 33746633380 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement
    • A. Binolfi, R.M. Rasia, C.W. Bertoncini, M. Ceolin, M. Zweckstetter, C. Griesinger, T.M. Jovin, and C.O. Fernandez Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement J. Am. Chem. Soc. 128 2006 9893 9901
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9893-9901
    • Binolfi, A.1    Rasia, R.M.2    Bertoncini, C.W.3    Ceolin, M.4    Zweckstetter, M.5    Griesinger, C.6    Jovin, T.M.7    Fernandez, C.O.8
  • 63
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein
    • D.P. Hong, A.L. Fink, and V.N. Uversky Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein J. Mol. Biol. 383 2008 214 223
    • (2008) J. Mol. Biol. , vol.383 , pp. 214-223
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3
  • 64
    • 78149459696 scopus 로고    scopus 로고
    • XLF regulates filament architecture of the XRCC4.ligase IV complex
    • M. Hammel, Y. Yu, S. Fang, S.P. Lees-Miller, and J.A. Tainer XLF regulates filament architecture of the XRCC4.ligase IV complex Structure 18 2010 1431 1442
    • (2010) Structure , vol.18 , pp. 1431-1442
    • Hammel, M.1    Yu, Y.2    Fang, S.3    Lees-Miller, S.P.4    Tainer, J.A.5
  • 66
    • 34547634446 scopus 로고    scopus 로고
    • From the cover: Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex
    • H. Tidow, and et al. From the cover: quaternary structures of tumor suppressor p53 and a specific p53 DNA complex Proc. Natl. Acad. Sci. U.S.A. 104 2007 12324 12329
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12324-12329
    • Tidow, H.1
  • 67
    • 66149161666 scopus 로고    scopus 로고
    • Intrinsic structural disorder of mouse proNGF
    • F. Paoletti, and et al. Intrinsic structural disorder of mouse proNGF Proteins 75 2009 990 1009
    • (2009) Proteins , vol.75 , pp. 990-1009
    • Paoletti, F.1
  • 68
    • 33646156874 scopus 로고    scopus 로고
    • The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured
    • M. Nardini, and et al. The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured Protein Sci. 15 2006 1042 1050
    • (2006) Protein Sci. , vol.15 , pp. 1042-1050
    • Nardini, M.1
  • 70
    • 79951571853 scopus 로고    scopus 로고
    • Different modes of interaction by TIAR and HuR with target RNA and DNA
    • H.S. Kim, and et al. Different modes of interaction by TIAR and HuR with target RNA and DNA Nucleic Acids Res. 39 2011 1117 1130
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1117-1130
    • Kim, H.S.1
  • 71
    • 0036777533 scopus 로고    scopus 로고
    • Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T
    • J. Li, V.N. Uversky, and A.L. Fink Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T Neurotoxicology 23 2002 553 567
    • (2002) Neurotoxicology , vol.23 , pp. 553-567
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 72
    • 0033539662 scopus 로고    scopus 로고
    • Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH
    • V.N. Uversky, and et al. Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH Biochemistry 38 1999 15009 15016
    • (1999) Biochemistry , vol.38 , pp. 15009-15016
    • Uversky, V.N.1
  • 73
    • 0034684969 scopus 로고    scopus 로고
    • Zn(2+)-mediated structure formation and compaction of the "natively unfolded" human prothymosin alpha
    • V.N. Uversky, and et al. Zn(2+)-mediated structure formation and compaction of the "natively unfolded" human prothymosin alpha Biochem. Biophys. Res. Commun. 267 2000 663 668
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 663-668
    • Uversky, V.N.1
  • 74
    • 79958773524 scopus 로고    scopus 로고
    • Structural memory of natively unfolded tau protein detected by small-angle X-ray scattering
    • A.V. Shkumatov, S. Chinnathambi, E. Mandelkow, and D.I. Svergun Structural memory of natively unfolded tau protein detected by small-angle X-ray scattering Proteins 79 2011 2122 2131
    • (2011) Proteins , vol.79 , pp. 2122-2131
    • Shkumatov, A.V.1    Chinnathambi, S.2    Mandelkow, E.3    Svergun, D.I.4
  • 75
    • 0035022941 scopus 로고    scopus 로고
    • Intrinsically disordered protein
    • A.K. Dunker, and et al. Intrinsically disordered protein J. Mol. Graph. Model. 19 2001 26 59
    • (2001) J. Mol. Graph. Model. , vol.19 , pp. 26-59
    • Dunker, A.K.1
  • 76
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • V.N. Uversky, J.R. Gillespie, and A.L. Fink Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41 2000 415 427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 77
    • 28444453002 scopus 로고    scopus 로고
    • Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data
    • A. Grishaev, J. Wu, J. Trewhella, and A. Bax Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data J. Am. Chem. Soc. 127 2005 16621 16628
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16621-16628
    • Grishaev, A.1    Wu, J.2    Trewhella, J.3    Bax, A.4
  • 78
    • 68049084850 scopus 로고    scopus 로고
    • Determination of multicomponent protein structures in solution using global orientation and shape restraints
    • J. Wang, and et al. Determination of multicomponent protein structures in solution using global orientation and shape restraints J. Am. Chem. Soc. 131 2009 10507 10515
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10507-10515
    • Wang, J.1
  • 79
    • 77956641793 scopus 로고    scopus 로고
    • Solution structure of the 128 kDa enzyme i dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering
    • C.D. Schwieters, J.Y. Suh, A. Grishaev, R. Ghirlando, Y. Takayama, and G.M. Clore Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering J. Am. Chem. Soc. 132 2010 13026 13045
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13026-13045
    • Schwieters, C.D.1    Suh, J.Y.2    Grishaev, A.3    Ghirlando, R.4    Takayama, Y.5    Clore, G.M.6
  • 80
    • 33947133083 scopus 로고    scopus 로고
    • Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure
    • J.A. Marsh, C. Neale, F.E. Jack, W.Y. Choy, A.Y. Lee, K.A. Crowhurst, and J.D. Forman-Kay Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure J. Mol. Biol. 367 2007 1494 1510
    • (2007) J. Mol. Biol. , vol.367 , pp. 1494-1510
    • Marsh, J.A.1    Neale, C.2    Jack, F.E.3    Choy, W.Y.4    Lee, A.Y.5    Crowhurst, K.A.6    Forman-Kay, J.D.7
  • 81
    • 67650684936 scopus 로고    scopus 로고
    • Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints
    • J.A. Marsh, and J.D. Forman-Kay Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints J. Mol. Biol. 391 2009 359 374
    • (2009) J. Mol. Biol. , vol.391 , pp. 359-374
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 83
    • 0028785802 scopus 로고
    • Prothymosin alpha: A biologically active protein with random coil conformation
    • K. Gast, and et al. Prothymosin alpha: a biologically active protein with random coil conformation Biochemistry 34 1995 13211 13218
    • (1995) Biochemistry , vol.34 , pp. 13211-13218
    • Gast, K.1
  • 84
    • 45749102885 scopus 로고    scopus 로고
    • Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: Application to the molecular recognition element of Sendai virus nucleoprotein
    • M.R. Jensen, K. Houben, E. Lescop, L. Blanchard, R.W. Ruigrok, and M. Blackledge Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein J. Am. Chem. Soc. 130 2008 8055 8061
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 8055-8061
    • Jensen, M.R.1    Houben, K.2    Lescop, E.3    Blanchard, L.4    Ruigrok, R.W.5    Blackledge, M.6
  • 85
    • 70450225410 scopus 로고    scopus 로고
    • The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module
    • C.Q. Schmidt, and et al. The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module J. Mol. Biol. 395 2010 105 122
    • (2010) J. Mol. Biol. , vol.395 , pp. 105-122
    • Schmidt, C.Q.1
  • 86
    • 10044296373 scopus 로고    scopus 로고
    • SAXS study of the PIR domain from the Grb14 molecular adaptor: A natively unfolded protein with a transient structure primer?
    • K. Moncoq, I. Broutin, C.T. Craescu, P. Vachette, A. Ducruix, and D. Durand SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer? Biophys. J. 87 2004 4056 4064
    • (2004) Biophys. J. , vol.87 , pp. 4056-4064
    • Moncoq, K.1    Broutin, I.2    Craescu, C.T.3    Vachette, P.4    Ducruix, A.5    Durand, D.6
  • 87
    • 33746605957 scopus 로고    scopus 로고
    • Structural insights into the interaction between prion protein and nucleic acid
    • L.M. Lima, and et al. Structural insights into the interaction between prion protein and nucleic acid Biochemistry 45 2006 9180 9187
    • (2006) Biochemistry , vol.45 , pp. 9180-9187
    • Lima, L.M.1
  • 88
    • 77956625350 scopus 로고    scopus 로고
    • Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X
    • X. Shi, and et al. Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X Biochem. J. 431 2010 93 102
    • (2010) Biochem. J. , vol.431 , pp. 93-102
    • Shi, X.1
  • 89
    • 77954256912 scopus 로고    scopus 로고
    • Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity
    • A. Garcia-Pino, and et al. Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity Cell 142 2010 101 111
    • (2010) Cell , vol.142 , pp. 101-111
    • Garcia-Pino, A.1
  • 92
    • 77952094752 scopus 로고    scopus 로고
    • Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering
    • P. Bernadó Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering Eur. Biophys. J. 39 2010 769 780
    • (2010) Eur. Biophys. J. , vol.39 , pp. 769-780
    • Bernadó, P.1
  • 95
    • 84891810469 scopus 로고    scopus 로고
    • PE-DB: A database of structural ensembles of intrinsically disordered and of unfolded proteins
    • M. Varadi, and et al. PE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins Nucleic Acids Res. 42 2014 D326 D335
    • (2014) Nucleic Acids Res. , vol.42 , pp. D326-D335
    • Varadi, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.