메뉴 건너뛰기




Volumn 89, Issue 1, 2005, Pages 619-634

Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; ARTICLE; DIFFUSION; EQUILIBRIUM CONSTANT; LAMM EQUATION MODELING; LIGAND BINDING; MATHEMATICAL ANALYSIS; MATHEMATICAL MODEL; MOLECULAR INTERACTION; PROBLEM SOLVING; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; REACTION ANALYSIS; SEDIMENTATION COEFFICIENT DISTRIBUTION; SEDIMENTATION RATE; ULTRACENTRIFUGATION;

EID: 20444380585     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.059568     Document Type: Article
Times cited : (158)

References (56)
  • 2
    • 0003159229 scopus 로고
    • Die differentialgleichung der ultrazentrifugierung
    • in German
    • Lamm, O. 1929. Die Differentialgleichung der Ultrazentrifugierung. Ark. Mat. Astr. Fys. 21B:1-4. [in German].
    • (1929) Ark. Mat. Astr. Fys. , vol.21 B , pp. 1-4
    • Lamm, O.1
  • 3
    • 0000198303 scopus 로고
    • An approximate solution to the Lamm equation
    • Holladay, L. A. 1979. An approximate solution to the Lamm equation. Biophys. Chem. 10:187-190.
    • (1979) Biophys. Chem. , vol.10 , pp. 187-190
    • Holladay, L.A.1
  • 4
    • 0019075659 scopus 로고
    • Ultracentrifuge studies of interactions and equilibria: Impact of interactive computer modelling
    • Gilbert, G. A., and L. M. Gilbert. 1980. Ultracentrifuge studies of interactions and equilibria: impact of interactive computer modelling. Biochem. Soc. Trans. 8:520-522.
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 520-522
    • Gilbert, G.A.1    Gilbert, L.M.2
  • 5
    • 0011203173 scopus 로고
    • Complete evaluation of sedimentation velocity experiments in the analytical ultracentrifuge
    • Urbanke, C., B. Ziegler, and K. Stieglitz. 1980. Complete evaluation of sedimentation velocity experiments in the analytical ultracentrifuge. Fresenius Z. Anal. Chem. 301:139-140.
    • (1980) Fresenius Z. Anal. Chem. , vol.301 , pp. 139-140
    • Urbanke, C.1    Ziegler, B.2    Stieglitz, K.3
  • 6
    • 0003094006 scopus 로고
    • Simulation of transport experiments for interacting systems
    • C. Frieden and L. W. Nichol, editors. Wiley, New York, NY
    • Cox, D. J., and R. S. Dale. 1981. Simulation of transport experiments for interacting systems. In Protein-Protein Interactions. C. Frieden and L. W. Nichol, editors. Wiley, New York, NY.
    • (1981) Protein-Protein Interactions
    • Cox, D.J.1    Dale, R.S.2
  • 7
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low molecular weight solutes
    • Philo, J. S. 1997. An improved function for fitting sedimentation velocity data for low molecular weight solutes. Biophys. J. 72:435-444.
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 9
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck, P. 1998. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75:1503-1512.
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 10
    • 0033949710 scopus 로고    scopus 로고
    • Determination of molecular parameters from sedimentation velocity experiments: Whole boundary fitting using approximate and numerical solutions of the Lamm equation
    • Demeler, B., J. Behlke, and O. Ristau. 2000. Determination of molecular parameters from sedimentation velocity experiments: whole boundary fitting using approximate and numerical solutions of the Lamm equation. Methods Enzymol. 321:36-66.
    • (2000) Methods Enzymol. , vol.321 , pp. 36-66
    • Demeler, B.1    Behlke, J.2    Ristau, O.3
  • 11
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by 36 sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • Stafford, W. F., and P. J. Sherwood. 2004. Analysis of heterologous interacting systems by 36 sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys. Chem. 108:231-243.
    • (2004) Biophys. Chem. , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 12
    • 0001209134 scopus 로고    scopus 로고
    • Analytical ultracentrifugation as a contemporary biomolecular research tool
    • Cole, J. L., and J. C. Hansen. 1999. Analytical ultracentrifugation as a contemporary biomolecular research tool. J. Biomol. Tech. 10:163-176.
    • (1999) J. Biomol. Tech. , vol.10 , pp. 163-176
    • Cole, J.L.1    Hansen, J.C.2
  • 13
    • 0032619228 scopus 로고    scopus 로고
    • Applications and future perspectives of analytical ultracentrifugation
    • Arisaka, F. 1999. Applications and future perspectives of analytical ultracentrifugation. Tanpakushitsu Kakusan Koso. 44:82-91.
    • (1999) Tanpakushitsu Kakusan Koso. , vol.44 , pp. 82-91
    • Arisaka, F.1
  • 15
    • 0032750872 scopus 로고    scopus 로고
    • Characterization of heterologous protein-protein interactions via analytical ultracentrifugation
    • Rivas, G., W. Stafford, and A. P. Minton. 1999. Characterization of heterologous protein-protein interactions via analytical ultracentrifugation. Methods. 19:194-212.
    • (1999) Methods , vol.19 , pp. 194-212
    • Rivas, G.1    Stafford, W.2    Minton, A.P.3
  • 16
    • 0036707991 scopus 로고    scopus 로고
    • Modem analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz, J., M. S. Lewis, and P. Schuck. 2002. Modem analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11:2067-2079.
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 17
    • 35448971602 scopus 로고    scopus 로고
    • A brief introduction to the analytical ultracentrifugation of proteins for beginners
    • D. J. Scott, S. E. Harding, and A. J. Rowe, editors. The Royal Society of Chemistry, Cambridge, UK. In press
    • Scott, D. J., and P. Schuck. 2005. A brief introduction to the analytical ultracentrifugation of proteins for beginners. In Modem Analytical Ultracentrifugation: Techniques and Methods. D. J. Scott, S. E. Harding, and A. J. Rowe, editors. The Royal Society of Chemistry, Cambridge, UK. In press.
    • (2005) Modem Analytical Ultracentrifugation: Techniques and Methods
    • Scott, D.J.1    Schuck, P.2
  • 18
    • 33644491645 scopus 로고    scopus 로고
    • Analytical ultracentrifugation in the study of protein self-association and heterogeneous protein-protein interactions
    • E. Golemis and P. D. Adams, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, NY. In press
    • Balbo, A., and P. Schuck. 2005. Analytical ultracentrifugation in the study of protein self-association and heterogeneous protein-protein interactions. In Protein-Protein Interactions. E. Golemis and P. D. Adams, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, NY. In press.
    • (2005) Protein-Protein Interactions
    • Balbo, A.1    Schuck, P.2
  • 20
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes
    • van Holde, K. E., and W. O. Weischet. 1978. Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes. Biopolymers. 17:1387-1403.
    • (1978) Biopolymers , vol.17 , pp. 1387-1403
    • Van Holde, K.E.1    Weischet, W.O.2
  • 21
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • Demeler, B., H. Saber, and J. C. Hansen. 1997. Identification and interpretation of complexity in sedimentation velocity boundaries. Biophys. J. 72:397-407.
    • (1997) Biophys. J. , vol.72 , pp. 397-407
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 22
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford, W. F. 1992. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203:295-301.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford, W.F.1
  • 23
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck, P., and P. Rossmanith. 2000. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers. 54:328-341.
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 24
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. 2000. Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78:1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 26
    • 11844293365 scopus 로고
    • Boundary problems in the sedimentation and electrophoresis of complex systems in rapid reversible equilibrium
    • Gilbert, G. A., and R. C. Jenkins. 1956. Boundary problems in the sedimentation and electrophoresis of complex systems in rapid reversible equilibrium. Nature. 177:853-854.
    • (1956) Nature , vol.177 , pp. 853-854
    • Gilbert, G.A.1    Jenkins, R.C.2
  • 27
    • 0008531095 scopus 로고
    • Reversible association processes of globular proteins. V. The study of associating systems by the methods of macromolecular physics
    • Steiner, R. F. 1954. Reversible association processes of globular proteins. V. The study of associating systems by the methods of macromolecular physics. Arch. Biochem. Biophys. 49:400-416.
    • (1954) Arch. Biochem. Biophys. , vol.49 , pp. 400-416
    • Steiner, R.F.1
  • 29
    • 84981860451 scopus 로고
    • Theory of sedimentation of interacting systems
    • Goad, W. B., and J. R. Cann. 1969. Theory of sedimentation of interacting systems. Ann. N. Y. Acad. Sci. 164:172-182.
    • (1969) Ann. N. Y. Acad. Sci. , vol.164 , pp. 172-182
    • Goad, W.B.1    Cann, J.R.2
  • 30
    • 0016702458 scopus 로고
    • Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations
    • Claverie, J.-M., H. Dreux, and R. Cohen. 1975. Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations. Biopolymers. 14:1685-1700.
    • (1975) Biopolymers , vol.14 , pp. 1685-1700
    • Claverie, J.-M.1    Dreux, H.2    Cohen, R.3
  • 31
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck, P. 2003. On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal. Biochem. 320:104-124.
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 32
    • 0016734742 scopus 로고
    • Equivalent and nonequivalent binding sites for tRNA on aminoacyl-tRNA synthetases
    • Krauss, G., A. Pingoud, D. Boehme, D. Riesner, F. Peters, and G. Maass. 1975. Equivalent and nonequivalent binding sites for tRNA on aminoacyl-tRNA synthetases. Eur. J. Biochem. 55:517-529.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 517-529
    • Krauss, G.1    Pingoud, A.2    Boehme, D.3    Riesner, D.4    Peters, F.5    Maass, G.6
  • 33
    • 21344438600 scopus 로고    scopus 로고
    • A sedimentation velocity method in the analytical ultracentrifuge for the study of protein-protein interactions
    • G. U. Nienhaus, editor. Humana Press, Totowa, NJ
    • Urbanke, C., G. Witte, and U. Curth. 2005. A sedimentation velocity method in the analytical ultracentrifuge for the study of protein-protein interactions. In Protein-Ligand Interactions: Methods and Applications. G. U. Nienhaus, editor. Humana Press, Totowa, NJ. 101-113.
    • (2005) Protein-Ligand Interactions: Methods and Applications , pp. 101-113
    • Urbanke, C.1    Witte, G.2    Curth, U.3
  • 34
    • 0035955727 scopus 로고    scopus 로고
    • ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously
    • Machner, M. P., C. Urbanke, M. Barzik, S. Otten, A. S. Sechi, J. Wehland, and D. W. Heinz. 2001. ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously. J. Biol. Chem. 276:40096-40103.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40096-40103
    • Machner, M.P.1    Urbanke, C.2    Barzik, M.3    Otten, S.4    Sechi, A.S.5    Wehland, J.6    Heinz, D.W.7
  • 35
    • 23244445215 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of protein-protein interactions: Sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory
    • J. Dam, and P. Schuck. 2005. Sedimentation velocity analysis of protein-protein interactions: sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory. Biophys. J. 89:651-666.
    • (2005) Biophys. J. , vol.89 , pp. 651-666
    • Dam, J.1    Schuck, P.2
  • 37
    • 84953600891 scopus 로고
    • A practical method for numerical evaluation of solutions of partial differential equations of the heat-conduction type
    • Crank, J., and P. Nicholson. 1947. A practical method for numerical evaluation of solutions of partial differential equations of the heat-conduction type. Proc. Cambridge Philos. Soc. 43:50-67.
    • (1947) Proc. Cambridge Philos. Soc. , vol.43 , pp. 50-67
    • Crank, J.1    Nicholson, P.2
  • 39
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck, P., M. A. Perugini, N. R. Gonzales, G. J. Howlett, and D. Schubert. 2002. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys. J. 82:1096-1111.
    • (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
  • 40
    • 36149035969 scopus 로고
    • Maximum entropy regularization of Fredholm integral equations of the first kind
    • Amato, U., and W. Hughes. 1991. Maximum entropy regularization of Fredholm integral equations of the first kind. Inverse problems 7:793-808.
    • (1991) Inverse Problems , vol.7 , pp. 793-808
    • Amato, U.1    Hughes, W.2
  • 41
    • 0033058274 scopus 로고    scopus 로고
    • Direct sedimentation analysis of interference optical data in analytical ultracentrifugation
    • Schuck, P., and B. Demeler. 1999. Direct sedimentation analysis of interference optical data in analytical ultracentrifugation. Biophys. J. 76:2288-2296.
    • (1999) Biophys. J. , vol.76 , pp. 2288-2296
    • Schuck, P.1    Demeler, B.2
  • 42
    • 1842428822 scopus 로고    scopus 로고
    • Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity profiles
    • Dam, J., and P. Schuck. 2004. Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity profiles. Methods Enzymol 384:185-212.
    • (2004) Methods Enzymol , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 43
    • 0014439427 scopus 로고
    • Computer simulation of sedimentation in the ultracentrifuge. IV. Velocity sedimentation of self-associating solutes
    • Cox, D. J. 1969. Computer simulation of sedimentation in the ultracentrifuge. IV. Velocity sedimentation of self-associating solutes. Arch. Biochem. Biophys. 129:106-123.
    • (1969) Arch. Biochem. Biophys. , vol.129 , pp. 106-123
    • Cox, D.J.1
  • 45
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson, L. E. 2002. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20:371-394.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 47
    • 0043199964 scopus 로고
    • Countercurrent distribution of chemically reacting systems. III. Analogs of moving boundary electrophoresis and sedimentation
    • Bethune, J. L., and G. Kegeles. 1961. Countercurrent distribution of chemically reacting systems. III. Analogs of moving boundary electrophoresis and sedimentation. J. Phys. Chem. 65:1761-1764.
    • (1961) J. Phys. Chem. , vol.65 , pp. 1761-1764
    • Bethune, J.L.1    Kegeles, G.2
  • 48
    • 84984088128 scopus 로고
    • Numerical simulations of the Lamm equation. III. Velocity centrifugation
    • Dishon, M., G. H. Weiss, and D. A. Yphantis. 1967. Numerical simulations of the Lamm equation. III. Velocity centrifugation. Biopolymers. 5:697-713.
    • (1967) Biopolymers , vol.5 , pp. 697-713
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 49
    • 0015922112 scopus 로고
    • Theory of electrophoresis and sedimentation for some kinetically controlled interactions
    • Cann, J. R., and D. C. Dates. 1973. Theory of electrophoresis and sedimentation for some kinetically controlled interactions. Biochemistry. 12:1112-1119.
    • (1973) Biochemistry , vol.12 , pp. 1112-1119
    • Cann, J.R.1    Dates, D.C.2
  • 50
    • 0022263777 scopus 로고
    • Effects of diffusion on the electrophoretic behavior of associating systems: The Gilbert-Jenkins theory revisited
    • Cann, J. R. 1985. Effects of diffusion on the electrophoretic behavior of associating systems: the Gilbert-Jenkins theory revisited. Arch. Biochem. Biophys. 240:489-499.
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 489-499
    • Cann, J.R.1
  • 51
    • 0031982612 scopus 로고    scopus 로고
    • Determination of molecular parameters by fitting sedimentation data to finite element solutions of the Lamm equation
    • Demeler, B., and H. Saber. 1998. Determination of molecular parameters by fitting sedimentation data to finite element solutions of the Lamm equation. Biophys. J. 74:444-454.
    • (1998) Biophys. J. , vol.74 , pp. 444-454
    • Demeler, B.1    Saber, H.2
  • 52
    • 0016243318 scopus 로고
    • Theory of sedimentation for kinetically controlled dimerization reactions
    • Cann, J. R., and G. Kegeles. 1974. Theory of sedimentation for kinetically controlled dimerization reactions. Biochemistry. 13:1868-1874.
    • (1974) Biochemistry , vol.13 , pp. 1868-1874
    • Cann, J.R.1    Kegeles, G.2
  • 53
    • 0020035883 scopus 로고
    • Theory of sedimentation for antigen-antibody reactions effect of antibody heterogeneity on the shape of the pattern
    • Cann, J. R. 1982. Theory of sedimentation for antigen-antibody reactions effect of antibody heterogeneity on the shape of the pattern. Mol. Immunol. 19:505-514.
    • (1982) Mol. Immunol. , vol.19 , pp. 505-514
    • Cann, J.R.1
  • 54
    • 0017673537 scopus 로고
    • Direct measurement of association constants for the binding of Escherichia coli lac repressor to non-operator DNA
    • Revzin, A., and P. H. von Hippel. 1977. Direct measurement of association constants for the binding of Escherichia coli lac repressor to non-operator DNA. Biochemistry. 16:4769-4776.
    • (1977) Biochemistry , vol.16 , pp. 4769-4776
    • Revzin, A.1    Von Hippel, P.H.2
  • 55
    • 0022484923 scopus 로고
    • Effects of microheterogeneity on sedimentation patterns of interacting proteins and the sedimentation behavior of systems involving two ligands
    • Cann, J. R. 1986. Effects of microheterogeneity on sedimentation patterns of interacting proteins and the sedimentation behavior of systems involving two ligands. Methods Enzymol. 130:19-35.
    • (1986) Methods Enzymol. , vol.130 , pp. 19-35
    • Cann, J.R.1
  • 56
    • 0024504918 scopus 로고
    • Analysis of the ligand-promoted global conformational change in aspartate trans-carbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments
    • Wemer, W. E., and H. K. Schachman. 1989. Analysis of the ligand-promoted global conformational change in aspartate trans-carbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments. J. Mol. Biol. 206:221-230.
    • (1989) J. Mol. Biol. , vol.206 , pp. 221-230
    • Wemer, W.E.1    Schachman, H.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.