메뉴 건너뛰기




Volumn 106, Issue 11, 2014, Pages 2474-2482

Probing the average local structure of biomolecules using small-angle scattering and scaling laws

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; INTRINSICALLY DISORDERED PROTEIN;

EID: 84901999651     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.03.050     Document Type: Article
Times cited : (9)

References (39)
  • 3
    • 84867048390 scopus 로고    scopus 로고
    • Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy
    • H. Hofmann, and A. Soranno B. Schuler Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy Proc. Natl. Acad. Sci. USA 109 2012 16155 16160
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16155-16160
    • Hofmann, H.1    Soranno, A.2    Schuler, B.3
  • 4
    • 0036401140 scopus 로고    scopus 로고
    • Toward a taxonomy of the denatured state: Small angle scattering studies of unfolded proteins
    • DOI 10.1016/S0065-3233(02)62009-1
    • I.S. Millett, S. Doniach, and K.W. Plaxco Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins Adv. Protein Chem. 62 2002 241 262 (Pubitemid 35204872)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 241-262
    • Millett, I.S.1    Doniach, S.2    Plaxco, K.W.3
  • 5
    • 0001296101 scopus 로고
    • Protein structure and polymer collapse
    • T. Dewey Protein structure and polymer collapse J. Phys. Chem. 98 1993 2250
    • (1993) J. Phys. Chem. , vol.98 , pp. 2250
    • Dewey, T.1
  • 6
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • R.P. Rambo, and J.A. Tainer Accurate assessment of mass, models and resolution by small-angle scattering Nature 496 2013 477 481
    • (2013) Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 8
    • 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
  • 9
    • 0026244044 scopus 로고
    • GNOM - A program package for small-angle scattering data processing
    • A.V. Semenyuk, and D.I. Svergun GNOM - a program package for small-angle scattering data processing J. Appl. Cryst. 24 1991 537 540
    • (1991) J. Appl. Cryst. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 10
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • O. Glatter A new method for the evaluation of small-angle scattering data J. Appl. Cryst. 10 1977 415 421
    • (1977) J. Appl. Cryst. , vol.10 , pp. 415-421
    • Glatter, O.1
  • 11
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • D. Svergun, and M. Koch Small-angle scattering studies of biological macromolecules in solution Rep. Prog. Phys. 66 2003 1735
    • (2003) Rep. Prog. Phys. , vol.66 , pp. 1735
    • Svergun, D.1    Koch, M.2
  • 13
    • 78651277458 scopus 로고    scopus 로고
    • A series of PDB-related databases for everyday needs
    • R.P. Joosten, and T.A. te Beek G. Vriend A series of PDB-related databases for everyday needs Nucleic Acids Res. 39 Database issue 2011 D411 D419
    • (2011) Nucleic Acids Res. , vol.39 , Issue.DATABASE ISSUE
    • Joosten, R.P.1    Te Beek, T.A.2    Vriend, G.3
  • 15
    • 77954280480 scopus 로고    scopus 로고
    • FOXS: A web server for rapid computation and fitting of SAXS profiles
    • D. Schneidman-Duhovny, M. Hammel, and A. Sali FOXS: a web server for rapid computation and fitting of SAXS profiles Nucleic Acids Res. 38 Web Server issue 2010 W540 W544
    • (2010) Nucleic Acids Res. , vol.38 , Issue.WEB SERVER ISSUE
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 16
    • 79958712678 scopus 로고    scopus 로고
    • Biophysical analysis and small-angle x-ray scattering-derived structures of MeCP2-nucleosome complexes
    • C. Yang, and M.J. van der Woerd 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    Luger, K.3
  • 17
    • 55949137920 scopus 로고    scopus 로고
    • Human regulatory protein Ki-1/57 has characteristics of an intrinsically unstructured protein
    • G.C. Bressan, and J.C. Silva J. Kobarg Human regulatory protein Ki-1/57 has characteristics of an intrinsically unstructured protein J. Proteome Res. 7 2008 4465 4474
    • (2008) J. Proteome Res. , vol.7 , pp. 4465-4474
    • Bressan, G.C.1    Silva, J.C.2    Kobarg, J.3
  • 19
    • 57749100291 scopus 로고    scopus 로고
    • Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems
    • A.D. Gazi, and M. Bastaki M. Kokkinidis Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems J. Biol. Chem. 283 2008 34062 34068
    • (2008) J. Biol. Chem. , vol.283 , pp. 34062-34068
    • Gazi, A.D.1    Bastaki, M.2    Kokkinidis, M.3
  • 20
    • 77955216637 scopus 로고    scopus 로고
    • Proline-rich salivary proteins have extended conformations
    • H. Boze, and T. Marlin B. Cabane Proline-rich salivary proteins have extended conformations Biophys. J. 99 2010 656 665
    • (2010) Biophys. J. , vol.99 , pp. 656-665
    • Boze, H.1    Marlin, T.2    Cabane, B.3
  • 21
    • 77955561331 scopus 로고    scopus 로고
    • Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1
    • Z. Lens, and F. Dewitte A. Verger Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1 Biochem. Biophys. Res. Commun. 399 2010 104 110
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 104-110
    • Lens, Z.1    Dewitte, F.2    Verger, A.3
  • 22
    • 77956304904 scopus 로고    scopus 로고
    • Human FEZ1 protein forms a disulfide bond mediated dimer: Implications for cargo transport
    • M.R. Alborghetti, and A.S. Furlan J. Kobarg Human FEZ1 protein forms a disulfide bond mediated dimer: implications for cargo transport J. Proteome Res. 9 2010 4595 4603
    • (2010) J. Proteome Res. , vol.9 , pp. 4595-4603
    • Alborghetti, M.R.1    Furlan, A.S.2    Kobarg, J.3
  • 24
    • 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?
    • DOI 10.1529/biophysj.104.048645
    • K. Moncoq, and I. Broutin 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 (Pubitemid 39602909)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 4056-4064
    • Moncoq, K.1    Broutin, I.2    Craescu, C.T.3    Vachette, P.4    Ducruix, A.5    Durand, D.6
  • 25
    • 79952149646 scopus 로고    scopus 로고
    • 0-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices
    • 0-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices Protein Sci. 20 2011 542 556
    • (2011) Protein Sci. , vol.20 , pp. 542-556
    • Leyrat, C.1    Jensen, M.R.2    Jamin, M.3
  • 26
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • D. Eliezer Biophysical characterization of intrinsically disordered proteins Curr. Opin. Struct. Biol. 19 2009 23 30
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 27
    • 82655179899 scopus 로고    scopus 로고
    • Structural analysis of intrinsically disordered proteins by small-angle x-ray scattering
    • P. Bernadó, 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
    • Bernadó, P.1    Svergun, D.I.2
  • 28
    • 77954256912 scopus 로고    scopus 로고
    • Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity
    • A. Garcia-Pino, and S. Balasubramanian R. Loris 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    Balasubramanian, S.2    Loris, R.3
  • 29
    • 84887975602 scopus 로고    scopus 로고
    • Small-angle neutron scattering study of a monoclonal antibody using free-energy constraints
    • N.J. Clark, and H. Zhang J.E. Curtis Small-angle neutron scattering study of a monoclonal antibody using free-energy constraints J. Phys. Chem. B 117 2013 14029 14038
    • (2013) J. Phys. Chem. B , vol.117 , pp. 14029-14038
    • Clark, N.J.1    Zhang, H.2    Curtis, J.E.3
  • 30
    • 72449188596 scopus 로고    scopus 로고
    • phox behaves in solution as a multidomain protein with semi-flexible linkers
    • phox behaves in solution as a multidomain protein with semi-flexible linkers J. Struct. Biol. 169 2010 45 53
    • (2010) J. Struct. Biol. , vol.169 , pp. 45-53
    • Durand, D.1    Vivès, C.2    Fieschi, F.3
  • 31
    • 84865525834 scopus 로고    scopus 로고
    • Integrative structural modeling with small angle x-ray scattering profiles
    • D. Schneidman-Duhovny, S.J. Kim, and A. Sali Integrative structural modeling with small angle x-ray scattering profiles BMC Struct. Biol. 12 2012 17
    • (2012) BMC Struct. Biol. , vol.12 , pp. 17
    • Schneidman-Duhovny, D.1    Kim, S.J.2    Sali, A.3
  • 33
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • DOI 10.1006/jmbi.1999.2829
    • J. Tsai, and R. Taylor M. Gerstein The packing density in proteins: standard radii and volumes J. Mol. Biol. 290 1999 253 266 (Pubitemid 29308589)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.1 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 34
    • 72049093998 scopus 로고    scopus 로고
    • A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering
    • P. Bernadó, 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
    • Bernadó, P.1    Blackledge, M.2
  • 35
    • 84857132923 scopus 로고    scopus 로고
    • How random are intrinsically disordered proteins? A small angle scattering perspective
    • V. Receveur-Brechot, and D. Durand How random are intrinsically disordered proteins? A small angle scattering perspective Curr. Protein Pept. Sci. 13 2012 55 75
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 55-75
    • Receveur-Brechot, V.1    Durand, D.2
  • 36
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • R.P. Rambo, and J.A. Tainer Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law Biopolymers 95 2011 559 571
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 38
    • 68349097394 scopus 로고    scopus 로고
    • Robust, high-throughput solution structural analyses by small angle x-ray scattering (SAXS)
    • G.L. Hura, and A.L. Menon J.A. Tainer 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    Menon, A.L.2    Tainer, J.A.3
  • 39
    • 12044253101 scopus 로고
    • SANS from homogeneous polymer mixtures: A unified overview
    • Springer New York
    • B. Hammouda SANS from homogeneous polymer mixtures: a unified overview Polymer Characteristics 1993 Springer New York 87 133
    • (1993) Polymer Characteristics , pp. 87-133
    • Hammouda, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.