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Volumn 326, Issue 2, 2004, Pages 234-256

Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition

Author keywords

Analytical ultracentrifugation; Heterogeneous association; Molar mass distribution; Protein complexes; Protein interactions

Indexed keywords

CENTRIFUGATION; CONSERVATION; MACROMOLECULES; MOLAR CONCENTRATION; MOLAR RATIO; PROTEINS; SEDIMENTATION;

EID: 1442274756     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.12.014     Document Type: Article
Times cited : (317)

References (61)
  • 3
    • 0025169221 scopus 로고
    • Quantitative characterization of reversible molecular associations via analytical ultracentrifugation
    • Minton A.P. Quantitative characterization of reversible molecular associations via analytical ultracentrifugation. Anal. Biochem. 190:1990;1-6.
    • (1990) Anal. Biochem. , vol.190 , pp. 1-6
    • Minton, A.P.1
  • 4
    • 0030272150 scopus 로고    scopus 로고
    • New revolutions in the evolution of analytical ultracentrifugation
    • Schuster T.M., Toedt J.M. New revolutions in the evolution of analytical ultracentrifugation. Curr. Opin. Struct. Biol. 6:1996;650-658.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 650-658
    • Schuster, T.M.1    Toedt, J.M.2
  • 5
    • 0030584676 scopus 로고    scopus 로고
    • Defining the structure and stability of macromolecular assemblies in solution: The re-emergence of analytical ultracentrifugation as a practical tool
    • Hensley P. Defining the structure and stability of macromolecular assemblies in solution: the re-emergence of analytical ultracentrifugation as a practical tool. Structure. 4:1996;367-373.
    • (1996) Structure , vol.4 , pp. 367-373
    • Hensley, P.1
  • 6
    • 44949135181 scopus 로고    scopus 로고
    • Analytical centrifugation: Equilibrium approach
    • Laue T.M. Analytical centrifugation: equilibrium approach. Curr. Protocols Protein Sci. 1999;20.3.1-20.3.13.
    • (1999) Curr. Protocols Protein Sci. , pp. 2031-20313
    • Laue, T.M.1
  • 8
    • 0032750872 scopus 로고    scopus 로고
    • Characterization of heterologous protein-protein interactions via analytical ultracentrifugation
    • Rivas G., Stafford W., Minton A.P. Characterization of heterologous protein-protein interactions via analytical ultracentrifugation. Methods. 19:1999;194-212.
    • (1999) Methods , vol.19 , pp. 194-212
    • Rivas, G.1    Stafford, W.2    Minton, A.P.3
  • 9
    • 0345073190 scopus 로고    scopus 로고
    • Analytical ultracentrifugation in the pharmaceutical industry
    • Liu J., Shire S.J. Analytical ultracentrifugation in the pharmaceutical industry. J. Pharm. Sci. 88:1999;1237-1241.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1237-1241
    • Liu, J.1    Shire, S.J.2
  • 10
    • 0032619228 scopus 로고    scopus 로고
    • Applications and future perspectives of analytical ultracentrifugation
    • Arisaka F. Applications and future perspectives of analytical ultracentrifugation. Tanpakushitsu Kakusan Koso. 44:1999;82-91.
    • (1999) Tanpakushitsu Kakusan Koso , vol.44 , pp. 82-91
    • Arisaka, F.1
  • 11
    • 0003747871 scopus 로고    scopus 로고
    • J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, & W. Strober. New York: Wiley
    • Schuck P., Braswell E.H. Coligan J.E., Kruisbeek A.M., Margulies D.H., Shevach E.M., Strober W. Current Protocols in Immunology. 2000;18.8.1-18.8.22 Wiley, New York.
    • (2000) Current Protocols in Immunology , pp. 1881-18822
    • Schuck, P.1    Braswell, E.H.2
  • 12
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz J., Lewis M.S., Schuck P. Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11:2002;2067-2079.
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 13
    • 0017107966 scopus 로고
    • Sedimentation equilibrium techniques: Multiple speed analyses and an overspeed procedure
    • Roark D.E. Sedimentation equilibrium techniques: multiple speed analyses and an overspeed procedure. Biophys. Chem. 5:1976;185-196.
    • (1976) Biophys. Chem. , vol.5 , pp. 185-196
    • Roark, D.E.1
  • 14
    • 0001826902 scopus 로고
    • On fitting exponentials by nonlinear least squares
    • Varah J.M. On fitting exponentials by nonlinear least squares. SIAM J. Sci. Stat. Comput. 6:1985;30-44.
    • (1985) SIAM J. Sci. Stat. Comput. , vol.6 , pp. 30-44
    • Varah, J.M.1
  • 17
    • 0033921410 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of mixed associations using numerical constraints to impose mass or signal conservation
    • Philo J.S. Sedimentation equilibrium analysis of mixed associations using numerical constraints to impose mass or signal conservation. Methods Enzymol. 321:2000;100-120.
    • (2000) Methods Enzymol. , vol.321 , pp. 100-120
    • Philo, J.S.1
  • 18
    • 0003300676 scopus 로고    scopus 로고
    • Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium
    • Minton A.P. Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium. Progr. Colloid Polym. Sci. 107:1997;11-19.
    • (1997) Progr. Colloid Polym. Sci. , vol.107 , pp. 11-19
    • Minton, A.P.1
  • 20
    • 0017116081 scopus 로고
    • The sedimentation equilibrium of heterogeneously associating systems and mixtures of non-interacting solutes: Analysis without determination of molecular weight averages
    • Nichol L.W., Jeffrey P.D., Milthorpe B.K. The sedimentation equilibrium of heterogeneously associating systems and mixtures of non-interacting solutes: analysis without determination of molecular weight averages. Biophys. Chem. 4:1976;259-267.
    • (1976) Biophys. Chem. , vol.4 , pp. 259-267
    • Nichol, L.W.1    Jeffrey, P.D.2    Milthorpe, B.K.3
  • 21
    • 0020475090 scopus 로고
    • Codon-induced transfer ribonucleic acid association: Quantitative analysis by sedimentation equilibrium
    • Pörschke D., Labuda D. Codon-induced transfer ribonucleic acid association: quantitative analysis by sedimentation equilibrium. Biochemistry. 21:1982;53-56.
    • (1982) Biochemistry , vol.21 , pp. 53-56
    • Pörschke, D.1    Labuda, D.2
  • 22
    • 0023001661 scopus 로고
    • Codon-induced association of the isolated anticodon loop of tRNA
    • Bujalowski W., Jung M., McLaughlin L.W., Pörschke D. Codon-induced association of the isolated anticodon loop of tRNA. Biochemistry. 25:1986;6372-6378.
    • (1986) Biochemistry , vol.25 , pp. 6372-6378
    • Bujalowski, W.1    Jung, M.2    McLaughlin, L.W.3    Pörschke, D.4
  • 23
    • 0023010495 scopus 로고
    • Ricin subunit association
    • Lewis M.S., Youle R.J. Ricin subunit association. J. Biol. Chem. 261:1986;11572-11577.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11572-11577
    • Lewis, M.S.1    Youle, R.J.2
  • 24
    • 0025801381 scopus 로고
    • The interaction of monomeric actin with two binding sites on acanthamoeba actobindin
    • Bubb M.R., Lewis M.S., Korn E.D. The interaction of monomeric actin with two binding sites on acanthamoeba actobindin. J. Biol. Chem. 266:1991;3820-3826.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3820-3826
    • Bubb, M.R.1    Lewis, M.S.2    Korn, E.D.3
  • 25
    • 0014259208 scopus 로고
    • Ultracentrifuge studies with Rayleigh interference optics. II. Low-speed sedimentation equilibrium of homogeneous systems
    • Richards E.G., Teller D.C., Schachman H.K. Ultracentrifuge studies with Rayleigh interference optics. II. Low-speed sedimentation equilibrium of homogeneous systems. Biochemistry. 7:1968;1054-1076.
    • (1968) Biochemistry , vol.7 , pp. 1054-1076
    • Richards, E.G.1    Teller, D.C.2    Schachman, H.K.3
  • 26
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis D.A. Equilibrium ultracentrifugation of dilute solutions. Biochemistry. 3:1964;297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 28
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. 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
  • 30
    • 0030041323 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction
    • Philo J.S., Aoki K.H., Arakawa T., Narhi L.O., Wen J. Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: one high-affinity and one low-affinity interaction. Biochemistry. 35:1996;1681-1691.
    • (1996) Biochemistry , vol.35 , pp. 1681-1691
    • Philo, J.S.1    Aoki, K.H.2    Arakawa, T.3    Narhi, L.O.4    Wen, J.5
  • 31
    • 0031051275 scopus 로고    scopus 로고
    • Dimerization of granulocyte-colony stimulating factor receptor: The Ig plus CRH construct of granulocyte-colony stimulating factor receptor forms a 2: 2 complex with a ligand
    • Horan T.P., Martin F., Simonet L., Arakawa T., Philo J.S. Dimerization of granulocyte-colony stimulating factor receptor: The Ig plus CRH construct of granulocyte-colony stimulating factor receptor forms a 2:2 complex with a ligand. J. Biochem. 121:1997;370-375.
    • (1997) J. Biochem. , vol.121 , pp. 370-375
    • Horan, T.P.1    Martin, F.2    Simonet, L.3    Arakawa, T.4    Philo, J.S.5
  • 32
    • 0035577805 scopus 로고    scopus 로고
    • A new data analysis method to determine binding constants of small molecules using equilibrium analytical ultracentrifugation with absorption optics
    • Arkin M., Lear J.D. A new data analysis method to determine binding constants of small molecules using equilibrium analytical ultracentrifugation with absorption optics. Anal. Biochem. 299:2001;98-107.
    • (2001) Anal. Biochem. , vol.299 , pp. 98-107
    • Arkin, M.1    Lear, J.D.2
  • 33
    • 0033058274 scopus 로고    scopus 로고
    • Direct sedimentation analysis of interference optical data in analytical ultracentrifugation
    • Schuck P., Demeler B. Direct sedimentation analysis of interference optical data in analytical ultracentrifugation. Biophys. J. 76:1999;2288-2296.
    • (1999) Biophys. J. , vol.76 , pp. 2288-2296
    • Schuck, P.1    Demeler, B.2
  • 35
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck P. 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
  • 36
    • 0017193835 scopus 로고
    • Inferring a molecular weight distribution, an ill-posed problem; And establishing the molecular weight scale using magnetic float techniques
    • Wiff D.R., Gehatia M.T. Inferring a molecular weight distribution, an ill-posed problem; and establishing the molecular weight scale using magnetic float techniques. Biophys. Chem. 5:1976;199-206.
    • (1976) Biophys. Chem. , vol.5 , pp. 199-206
    • Wiff, D.R.1    Gehatia, M.T.2
  • 37
    • 84890326874 scopus 로고
    • A technique for the numerical solution of certain integral equations of the first kind
    • Phillips D.L. A technique for the numerical solution of certain integral equations of the first kind. Assoc. Comput. Mach. 9:1962;84-97.
    • (1962) Assoc. Comput. Mach. , vol.9 , pp. 84-97
    • Phillips, D.L.1
  • 38
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher S.W. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comp. Phys. Commun. 27:1982;213-227.
    • (1982) Comp. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 39
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck P., Rossmanith P. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers. 54:2000;328-341.
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 40
    • 0038778441 scopus 로고    scopus 로고
    • Combined affinity and rate constant distributions of ligand populations from experimental surface-binding kinetics and equilibria
    • Svitel J., Balbo A., Mariuzza R.A., Gonzales N.R., Schuck P. Combined affinity and rate constant distributions of ligand populations from experimental surface-binding kinetics and equilibria. Biophys. J. 84:2003;4062-4077.
    • (2003) Biophys. J. , vol.84 , pp. 4062-4077
    • Svitel, J.1    Balbo, A.2    Mariuzza, R.A.3    Gonzales, N.R.4    Schuck, P.5
  • 41
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P., Perugini M.A., Gonzales N.R., Howlett G.J., Schubert D. 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
  • 43
    • 0027410312 scopus 로고
    • Rapid and accurate microfractionation of the contents of small centrifuge tubes: Application in the measurement of molecular weights of proteins via sedimentation equilibrium
    • Darawshe S., Rivas G., Minton A.P. Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weights of proteins via sedimentation equilibrium. Anal. Biochem. 209:1993;130-135.
    • (1993) Anal. Biochem. , vol.209 , pp. 130-135
    • Darawshe, S.1    Rivas, G.2    Minton, A.P.3
  • 45
    • 1442339409 scopus 로고    scopus 로고
    • A model for sedimentation in inhomogeneous media. II. Compressibility of aqueous and organic solvens
    • in press
    • P. Schuck, A model for sedimentation in inhomogeneous media. II. Compressibility of aqueous and organic solvens, Biophys. Chem. (2003), in press
    • (2003) Biophys. Chem.
    • Schuck, P.1
  • 46
    • 0014761021 scopus 로고
    • Improved ultracentrifuge cells for high-speed sedimentation equilibrium studies with interference optics
    • Ansevin A.T., Roark D.E., Yphantis D.A. Improved ultracentrifuge cells for high-speed sedimentation equilibrium studies with interference optics. Anal. Biochem. 34:1970;237-261.
    • (1970) Anal. Biochem. , vol.34 , pp. 237-261
    • Ansevin, A.T.1    Roark, D.E.2    Yphantis, D.A.3
  • 48
    • 0023664830 scopus 로고
    • Sedimentation equilibrium measurements of recombinant DNA derived human interferon gamma
    • Yphantis D.A., Arakawa T. Sedimentation equilibrium measurements of recombinant DNA derived human interferon gamma. Biochemistry. 26:1987;5422-5427.
    • (1987) Biochemistry , vol.26 , pp. 5422-5427
    • Yphantis, D.A.1    Arakawa, T.2
  • 49
    • 0029077350 scopus 로고
    • The effect of pH and temperature on the self-association of recombinant human interleukin-2 as studied by equilibrium sedimentation
    • Advant S.J., Braswell E.H., Kumar C.V., Kalonia D.S. The effect of pH and temperature on the self-association of recombinant human interleukin-2 as studied by equilibrium sedimentation. Pharm. Res. 12:1995;637-641.
    • (1995) Pharm. Res. , vol.12 , pp. 637-641
    • Advant, S.J.1    Braswell, E.H.2    Kumar, C.V.3    Kalonia, D.S.4
  • 50
    • 0036634873 scopus 로고    scopus 로고
    • Analysis of a temperature-sensitive mutant rotavirus indicates that NSP2 octamers are the functional form of the protein
    • Taraporewala Z.F., Schuck P., Ramig R.F., Silvestri L., Patton J.T. Analysis of a temperature-sensitive mutant rotavirus indicates that NSP2 octamers are the functional form of the protein. J. Virol. 76:2002;7082-7093.
    • (2002) J. Virol. , vol.76 , pp. 7082-7093
    • Taraporewala, Z.F.1    Schuck, P.2    Ramig, R.F.3    Silvestri, L.4    Patton, J.T.5
  • 53
    • 0000426466 scopus 로고
    • Molecular weights and molecular weight distribution of polymers by equilibrium ultracentrifugation. Part II. Molecular weight distribution
    • Scholte T.G. Molecular weights and molecular weight distribution of polymers by equilibrium ultracentrifugation. Part II. Molecular weight distribution. J. Polym. Sci. 6:1968;111-127.
    • (1968) J. Polym. Sci. , vol.6 , pp. 111-127
    • Scholte, T.G.1
  • 54
    • 0017107967 scopus 로고
    • Molecular weights and molecular-weight distributions from ultracentrifugation of nonideal solutions
    • Wan P.J., Adams E.T. Molecular weights and molecular-weight distributions from ultracentrifugation of nonideal solutions. Biophys. Chem. 5:1976;207-241.
    • (1976) Biophys. Chem. , vol.5 , pp. 207-241
    • Wan, P.J.1    Adams, E.T.2
  • 57
    • 0033179805 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of interference optical data by systematic noise decomposition
    • Schuck P. Sedimentation equilibrium analysis of interference optical data by systematic noise decomposition. Anal. Biochem. 272:1999;199-208.
    • (1999) Anal. Biochem. , vol.272 , pp. 199-208
    • Schuck, P.1
  • 58
    • 0001095730 scopus 로고
    • Ultracentrifuge studies with Rayleigh interference optics. I. General applications
    • Richards E.G., Schachman H.K. Ultracentrifuge studies with Rayleigh interference optics. I. General applications. J. Phys. Chem. 63:1959;1578-1591.
    • (1959) J. Phys. Chem. , vol.63 , pp. 1578-1591
    • Richards, E.G.1    Schachman, H.K.2
  • 59
    • 0014216034 scopus 로고
    • Simultaneous determination of partial specific volumes and molecular weights with microgram quantities
    • Edelstein J., Schachman H. Simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J. Biol. Chem. 242:1967;306-311.
    • (1967) J. Biol. Chem. , vol.242 , pp. 306-311
    • Edelstein, J.1    Schachman, H.2
  • 60
    • 0043166158 scopus 로고    scopus 로고
    • Direct analysis of protein sedimentation equilibrium in detergent solutions without density matching
    • Noy D., Calhoun J.R., Lear J.D. Direct analysis of protein sedimentation equilibrium in detergent solutions without density matching. Anal. Biochem. 320:2003;185-192.
    • (2003) Anal. Biochem. , vol.320 , pp. 185-192
    • Noy, D.1    Calhoun, J.R.2    Lear, J.D.3


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