메뉴 건너뛰기




Volumn 437, Issue 1, 2013, Pages 104-108

Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation

Author keywords

Hydrodynamic modeling; Sedimentation velocity

Indexed keywords

DATA ACQUISITION; HYDRODYNAMICS; UNCERTAINTY ANALYSIS;

EID: 84876134886     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.02.011     Document Type: Article
Times cited : (97)

References (30)
  • 1
    • 0031647711 scopus 로고
    • Analytical ultracentrifugation from 1924 to the present: A remarkable history
    • K.E. Van Holde, and J.C. Hansen Analytical ultracentrifugation from 1924 to the present: a remarkable history Chemtracts Biochem. Mol. Biol. 11 1998 1924 933 943
    • (1924) Chemtracts Biochem. Mol. Biol. , vol.11 , Issue.1998 , pp. 933-943
    • Van Holde, K.E.1    Hansen, J.C.2
  • 2
    • 0002151801 scopus 로고
    • Is there a future for the ultracentrifuge?
    • S.E. Harding, A.J. Rowe, J.C. Horton, Royal Society of Chemistry Cambridge, UK
    • H.K. Schachman Is there a future for the ultracentrifuge? S.E. Harding, A.J. Rowe, J.C. Horton, Analytical Ultracentrifugation in Biochemistry and Polymer Science 1992 Royal Society of Chemistry Cambridge, UK 3 15
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 3-15
    • Schachman, H.K.1
  • 3
  • 6
    • 84865983441 scopus 로고
    • Exploring cells with a centrifuge
    • C. De Duve, Exploring cells with a centrifuge, Nobel Lecture (1974). < http://www.nobelprize.org/nobel-prizes/medicine/laureates/1974/duve-lecture. html >.
    • (1974) Nobel Lecture
    • De Duve, C.1
  • 7
    • 79955607619 scopus 로고    scopus 로고
    • Editorial for the special issue of methods, "modern analytical ultracentrifugation"
    • P. Schuck, and H. Zhao Editorial for the special issue of methods, "modern analytical ultracentrifugation" Methods 54 2011 1 3
    • (2011) Methods , vol.54 , pp. 1-3
    • Schuck, P.1    Zhao, H.2
  • 8
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • G.J. Howlett, A.P. Minton, and G. Rivas Analytical ultracentrifugation for the study of protein association and assembly Curr. Opin. Chem. Biol. 10 2006 430 436
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3
  • 9
    • 79955634085 scopus 로고    scopus 로고
    • Measuring low levels of protein aggregation by sedimentation velocity
    • J.P. Gabrielson, and K.K. Arthur Measuring low levels of protein aggregation by sedimentation velocity Methods 54 2011 83 91
    • (2011) Methods , vol.54 , pp. 83-91
    • Gabrielson, J.P.1    Arthur, K.K.2
  • 10
    • 84869444250 scopus 로고    scopus 로고
    • Validity range of centrifuges for the regulation of nanomaterials: From classification to as-tested coronas
    • W. Wohlleben Validity range of centrifuges for the regulation of nanomaterials: from classification to as-tested coronas J. Nanopart. Res. 14 2012 1300
    • (2012) J. Nanopart. Res. , vol.14 , pp. 1300
    • Wohlleben, W.1
  • 11
    • 0042358855 scopus 로고    scopus 로고
    • Probing conformation and conformational change in proteins is optimally undertaken in relative mode
    • N. Errington, and A.J. Rowe Probing conformation and conformational change in proteins is optimally undertaken in relative mode Eur. Biophys. J. 32 2003 511 517
    • (2003) Eur. Biophys. J. , vol.32 , pp. 511-517
    • Errington, N.1    Rowe, A.J.2
  • 12
    • 0030793359 scopus 로고    scopus 로고
    • The ELLIPS suite of macromolecular conformation algorithms
    • S.E. Harding, J.C. Horton, and H. Cölfen The ELLIPS suite of macromolecular conformation algorithms Eur. Biophys. J. 25 1997 347 359
    • (1997) Eur. Biophys. J. , vol.25 , pp. 347-359
    • Harding, S.E.1    Horton, J.C.2    Cölfen, H.3
  • 13
    • 0019526265 scopus 로고
    • Hydrodynamic properties of complex, rigid, biological macromolecules: Theory and applications
    • J.G. Garcia de la Torre, and V.A. Bloomfield Hydrodynamic properties of complex, rigid, biological macromolecules: theory and applications Q. Rev. Biophys. 14 1981 81 139
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 81-139
    • Garcia De La Torre, J.G.1    Bloomfield, V.A.2
  • 14
    • 33748451514 scopus 로고    scopus 로고
    • Precise boundary element computation of protein transport properties: Diffusion tensors, specific volume, and hydration
    • S.R. Aragon, and D.K. Hahn Precise boundary element computation of protein transport properties: diffusion tensors, specific volume, and hydration Biophys. J. 91 2006 1591 1603
    • (2006) Biophys. J. , vol.91 , pp. 1591-1603
    • Aragon, S.R.1    Hahn, D.K.2
  • 15
    • 79955580820 scopus 로고    scopus 로고
    • Analytical ultracentrifugation combined with X-ray and neutron scattering: Experiment and modelling
    • S.J. Perkins, R. Nan, K. Li, S. Khan, and Y. Abe Analytical ultracentrifugation combined with X-ray and neutron scattering: experiment and modelling Methods 54 2011 181 199
    • (2011) Methods , vol.54 , pp. 181-199
    • Perkins, S.J.1    Nan, R.2    Li, K.3    Khan, S.4    Abe, Y.5
  • 16
    • 84879936868 scopus 로고    scopus 로고
    • Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation
    • H. Zhao, C.A. Brautigam, R. Ghirlando, and P. Schuck Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation Curr. Protoc. Protein Sci. 7 2013 20.12.1
    • (2013) Curr. Protoc. Protein Sci. , vol.7 , pp. 20121
    • Zhao, H.1    Brautigam, C.A.2    Ghirlando, R.3    Schuck, P.4
  • 17
    • 57549085173 scopus 로고    scopus 로고
    • Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation
    • P.H. Brown, A. Balbo, and P. Schuck Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation Curr. Protoc. Immunol. 18 2008 18.15
    • (2008) Curr. Protoc. Immunol. , vol.18 , pp. 1815
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3
  • 18
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 19
    • 70349696256 scopus 로고    scopus 로고
    • On the analysis of sedimentation velocity in the study of protein complexes
    • P.H. Brown, A. Balbo, and P. Schuck On the analysis of sedimentation velocity in the study of protein complexes Eur. Biophys. J. 38 2009 1079 1099
    • (2009) Eur. Biophys. J. , vol.38 , pp. 1079-1099
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3
  • 20
    • 0035971072 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes
    • P. Schuck, Z.F. Taraporewala, P. McPhie, and J.T. Patton Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes J. Biol. Chem. 276 2001 9679 9687
    • (2001) J. Biol. Chem. , vol.276 , pp. 9679-9687
    • Schuck, P.1    Taraporewala, Z.F.2    McPhie, P.3    Patton, J.T.4
  • 22
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • P. Schuck, M.A. Perugini, N.R. Gonzales, G.J. Howlett, and D. Schubert Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems Biophys. J. 82 2002 1096 1111
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 23
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • P. Schuck On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation Anal. Biochem. 320 2003 104 124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 24
    • 79955638852 scopus 로고    scopus 로고
    • The boundary structure in the analysis of reversibly interacting systems by sedimentation velocity
    • H. Zhao, A. Balbo, P.H. Brown, and P. Schuck The boundary structure in the analysis of reversibly interacting systems by sedimentation velocity Methods 54 2011 16 30
    • (2011) Methods , vol.54 , pp. 16-30
    • Zhao, H.1    Balbo, A.2    Brown, P.H.3    Schuck, P.4
  • 25
    • 79955609636 scopus 로고    scopus 로고
    • Using Lamm equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions
    • C.A. Brautigam Using Lamm equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions Methods 54 2011 4 15
    • (2011) Methods , vol.54 , pp. 4-15
    • Brautigam, C.A.1
  • 26
    • 20444380585 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)
    • J. Dam, C.A. Velikovsky, R. Mariuzza, C. Urbanke, and P. Schuck Sedimentation velocity analysis of protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s) Biophys. J. 89 2005 619 634
    • (2005) Biophys. J. , vol.89 , pp. 619-634
    • Dam, J.1    Velikovsky, C.A.2    Mariuzza, R.3    Urbanke, C.4    Schuck, P.5
  • 27
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium, and kinetic constants
    • W.F. Stafford, and P.J. Sherwood Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium, and kinetic constants Biophys. Chem. 108 2004 231 243
    • (2004) Biophys. Chem. , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 28
    • 0017693590 scopus 로고
    • Allosteric regulation of aspartate transcarbamoylase: Analysis of the structural and functional behavior in terms of a two-state model
    • G.J. Howlett, M.N. Blackburn, J.G. Compton, and H.K. Schachman Allosteric regulation of aspartate transcarbamoylase: analysis of the structural and functional behavior in terms of a two-state model Biochemistry 16 1977 5091 5099
    • (1977) Biochemistry , vol.16 , pp. 5091-5099
    • Howlett, G.J.1    Blackburn, M.N.2    Compton, J.G.3    Schachman, H.K.4
  • 30
    • 79955639129 scopus 로고    scopus 로고
    • Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity
    • S.B. Padrick, and C.A. Brautigam Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity Methods 54 2011 39 55
    • (2011) Methods , vol.54 , pp. 39-55
    • Padrick, S.B.1    Brautigam, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.