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Volumn 108, Issue 1-3, 2004, Pages 201-214

A model for sedimentation in inhomogeneous media. II. Compressibility of aqueous and organic solvents

Author keywords

Analytical ultracentrifugation; Compressible solvents; Density gradient centrifugation; Finite element methods; Lamm equation; Polymers; Sedimentation velocity; Size distributions

Indexed keywords

ORGANIC SOLVENT; WATER;

EID: 1642364826     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2003.10.017     Document Type: Article
Times cited : (32)

References (61)
  • 3
    • 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: Companion Methods Enzymol. 19:1999;194-212.
    • (1999) Methods: Companion Methods Enzymol. , vol.19 , pp. 194-212
    • Rivas, G.1    Stafford, W.2    Minton, A.P.3
  • 4
    • 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
  • 5
    • 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
  • 7
    • 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
  • 8
    • 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
  • 10
    • 0030607048 scopus 로고    scopus 로고
    • Comparison of diffusion coefficients obtained from ternary polymer solutions using dynamic light scattering and ultracentrifugation
    • Pinder D.N., Ueleni T., Lewis J.A. Comparison of diffusion coefficients obtained from ternary polymer solutions using dynamic light scattering and ultracentrifugation. J. Mol. Struct. 383:1996;107-115.
    • (1996) J. Mol. Struct. , vol.383 , pp. 107-115
    • Pinder, D.N.1    Ueleni, T.2    Lewis, J.A.3
  • 11
  • 12
    • 0032964389 scopus 로고    scopus 로고
    • Characterizing the solution properties of supramolecular systems by analytical ultracentrifugation
    • Schubert D., Tziatzios C., Schuck P., Schubert U.S. Characterizing the solution properties of supramolecular systems by analytical ultracentrifugation. Chem. Eur. J. 5:1999;1377-1383.
    • (1999) Chem. Eur. J. , vol.5 , pp. 1377-1383
    • Schubert, D.1    Tziatzios, C.2    Schuck, P.3    Schubert, U.S.4
  • 15
    • 33846302079 scopus 로고
    • Equilibrium sedimentation of macromolecules and viruses in a density gradient
    • Vinograd J., Hearst J.E. Equilibrium sedimentation of macromolecules and viruses in a density gradient. Fortschr. Chem. Org. Nat. 20:1962;372-422.
    • (1962) Fortschr. Chem. Org. Nat. , vol.20 , pp. 372-422
    • Vinograd, J.1    Hearst, J.E.2
  • 19
    • 1642394636 scopus 로고
    • The effect of pressure on sedimentation, and compressibility measurements in the ultracentrifuge
    • Cheng P.Y., Schachman H.K. The effect of pressure on sedimentation, and compressibility measurements in the ultracentrifuge. J. Am. Chem. Soc. 77:1954;1498-1501.
    • (1954) J. Am. Chem. Soc. , vol.77 , pp. 1498-1501
    • Cheng, P.Y.1    Schachman, H.K.2
  • 20
    • 0000115930 scopus 로고
    • Ultracentrifuge studies with absorption optics. I. An automatic photoelectric scanning absorption system
    • Hanlon S., Lamers K., Lauterbach G., Johnson R., Schachman H.K. Ultracentrifuge studies with absorption optics. I. An automatic photoelectric scanning absorption system. Arch. Biochem. Biophys. 99:1962;157-174.
    • (1962) Arch. Biochem. Biophys. , vol.99 , pp. 157-174
    • Hanlon, S.1    Lamers, K.2    Lauterbach, G.3    Johnson, R.4    Schachman, H.K.5
  • 22
    • 0020554475 scopus 로고
    • Rapid precision interferometry for the analytical ultracentrifuge. I. A laser controller based on a phase-lock-loop circuit
    • Laue T.M., Domanik R.A., Yphantis D.A. Rapid precision interferometry for the analytical ultracentrifuge. I. A laser controller based on a phase-lock-loop circuit. Anal. Biochem. 131:1983;220-231.
    • (1983) Anal. Biochem. , vol.131 , pp. 220-231
    • Laue, T.M.1    Domanik, R.A.2    Yphantis, D.A.3
  • 23
    • 0021764697 scopus 로고
    • Rapid precision interferometry for the analytical ultracentrifuge. II. A laser controller based on a rate-multiplying circuit
    • Yphantis D.A., Laue T.M., Anderson I. Rapid precision interferometry for the analytical ultracentrifuge. II. A laser controller based on a rate-multiplying circuit. Anal. Biochem. 143:1984;95-102.
    • (1984) Anal. Biochem. , vol.143 , pp. 95-102
    • Yphantis, D.A.1    Laue, T.M.2    Anderson, I.3
  • 24
    • 0028125516 scopus 로고
    • An on-line interferometer for the XL-A ultracentrifuge
    • Laue T.M. An on-line interferometer for the XL-A ultracentrifuge. Prog. Coll. Polym. Sci. 94:1994;74-81.
    • (1994) Prog. Coll. Polym. Sci. , vol.94 , pp. 74-81
    • Laue, T.M.1
  • 25
    • 0003159229 scopus 로고
    • Die Differentialgleichung der Ultrazentrifugierung
    • Lamm O. Die Differentialgleichung der Ultrazentrifugierung. Ark. Mat. Astr. Fys., Part B. 21:(2):1929;1-4.
    • (1929) Ark. Mat. Astr. Fys., Part B , vol.21 , Issue.2 , pp. 1-4
    • Lamm, O.1
  • 26
    • 0016702458 scopus 로고
    • Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations
    • Claverie J.-M., Dreux H., Cohen R. Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations. Biopolymers. 14:1975;1685-1700.
    • (1975) Biopolymers , vol.14 , pp. 1685-1700
    • Claverie, J.-M.1    Dreux, H.2    Cohen, R.3
  • 27
    • 0000198303 scopus 로고
    • An approximate solution to the Lamm equation
    • Holladay L.A. An approximate solution to the Lamm equation. Biophys. Chem. 10:1979;187-190.
    • (1979) Biophys. Chem. , vol.10 , pp. 187-190
    • Holladay, L.A.1
  • 28
    • 0016243318 scopus 로고
    • Theory of sedimentation for kinetically controlled dimerization reactions
    • Cann J.R., Kegeles G. Theory of sedimentation for kinetically controlled dimerization reactions. Biochemistry. 13:1974;1868-1874.
    • (1974) Biochemistry , vol.13 , pp. 1868-1874
    • Cann, J.R.1    Kegeles, G.2
  • 30
    • 0008566463 scopus 로고
    • General solution to the inverse problem of the differential equation of the ultracentrifuge
    • Todd G.P., Haschemeyer R.H. General solution to the inverse problem of the differential equation of the ultracentrifuge. Proc. Natl. Acad. Sci. USA. 78:1981;6739-6743.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6739-6743
    • Todd, G.P.1    Haschemeyer, R.H.2
  • 31
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low molecular weight solutes
    • Philo J.S. An improved function for fitting sedimentation velocity data for low molecular weight solutes. Biophys. J. 72:1997;435-444.
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 32
    • 0037160547 scopus 로고    scopus 로고
    • A new approximate whole boundary solution of the Lamm differential equation for the analysis of sedimentation velocity experiments
    • Behlke J., Ristau O. A new approximate whole boundary solution of the Lamm differential equation for the analysis of sedimentation velocity experiments. Biophys. Chem. 95:2002;59-68.
    • (2002) Biophys. Chem. , vol.95 , pp. 59-68
    • Behlke, J.1    Ristau, O.2
  • 33
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck P. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75:1998;1503-1512.
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 34
    • 0031962095 scopus 로고    scopus 로고
    • Determination of sedimentation coefficients for small peptides
    • Schuck P., MacPhee C.E., Howlett G.J. Determination of sedimentation coefficients for small peptides. Biophys. J. 74:1998;466-474.
    • (1998) Biophys. J. , vol.74 , pp. 466-474
    • Schuck, P.1    MacPhee, C.E.2    Howlett, G.J.3
  • 35
    • 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
  • 36
    • 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
  • 38
    • 18744407250 scopus 로고    scopus 로고
    • Differences in the binding capacity of human apolipoprotein E3 and E4 to size-fractionated lipid emulsions
    • Perugini M.A., Schuck P., Howlett G.J. Differences in the binding capacity of human apolipoprotein E3 and E4 to size-fractionated lipid emulsions. Eur. J. Biochem. 269:2002;5939-5949.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5939-5949
    • Perugini, M.A.1    Schuck, P.2    Howlett, G.J.3
  • 39
    • 0034620517 scopus 로고    scopus 로고
    • Insights into the molecular relationships between malate and lactate dehydrogenases: Structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui
    • Madern D., Ebel C., Mevarech M., Richard S.B., Pfister C., Zaccai G. Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui. Biochemistry. 39:2000;1001-1010.
    • (2000) Biochemistry , vol.39 , pp. 1001-1010
    • Madern, D.1    Ebel, C.2    Mevarech, M.3    Richard, S.B.4    Pfister, C.5    Zaccai, G.6
  • 40
    • 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
  • 41
    • 0034581366 scopus 로고    scopus 로고
    • M.L. Johnson, J.N. Abelson, & M.I. Simon. New York: Academic Press
    • Stafford W.F. Johnson M.L., Abelson J.N., Simon M.I. Methods Enzymol, vol. 323. 2000;302-325 Academic Press, New York.
    • (2000) Methods Enzymol, Vol. 323 , pp. 302-325
    • Stafford, W.F.1
  • 42
    • 0034816707 scopus 로고    scopus 로고
    • Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents
    • Solovyova A., Schuck P., Costenaro L., Ebel C. Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents. Biophys. J. 81:2001;1868-1880.
    • (2001) Biophys. J. , vol.81 , pp. 1868-1880
    • Solovyova, A.1    Schuck, P.2    Costenaro, L.3    Ebel, C.4
  • 43
    • 1642293193 scopus 로고    scopus 로고
    • A model for sedimentation in homogeneous media. I. Dynamic density gradients from sedimenting co-solutes
    • Schuck P. A model for sedimentation in homogeneous media. I. Dynamic density gradients from sedimenting co-solutes. Biophys. Chem. 108:2004;187-200.
    • (2004) Biophys. Chem. , vol.108 , pp. 187-200
    • Schuck, P.1
  • 44
    • 1642297076 scopus 로고
    • Effects of hydrostatic pressure upon sedimentation in the ultracentrifuge
    • Fujita H. Effects of hydrostatic pressure upon sedimentation in the ultracentrifuge. J. Am. Chem. Soc. 78:1956;3598-3604.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 3598-3604
    • Fujita, H.1
  • 45
    • 84982335864 scopus 로고
    • Ultrazentrifugale Polydispersitätsbestimmungen an hochpolymeren Stoffen
    • Signer R., Gross H. Ultrazentrifugale Polydispersitätsbestimmungen an hochpolymeren Stoffen. Helv. Chim. Acta. 17:1934;726.
    • (1934) Helv. Chim. Acta , vol.17 , pp. 726
    • Signer, R.1    Gross, H.2
  • 46
    • 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. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203:1992;295-301.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford, W.F.1
  • 47
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo J.S. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279:2000;151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 48
    • 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
  • 49
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes
    • van Holde K.E., Weischet W.O. Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes. Biopolymers. 17:1978;1387-1403.
    • (1978) Biopolymers , vol.17 , pp. 1387-1403
    • Van Holde, K.E.1    Weischet, W.O.2
  • 50
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • Demeler B., Saber H., Hansen J.C. Identification and interpretation of complexity in sedimentation velocity boundaries. Biophys. J. 72:1997;397-407.
    • (1997) Biophys. J. , vol.72 , pp. 397-407
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 51
    • 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
  • 53
    • 33947564029 scopus 로고
    • A contribution to the knowledge of some physico-chemical properties of polystyrene
    • Gralén N., Lagermalm G. A contribution to the knowledge of some physico-chemical properties of polystyrene. J. Phys. Chem. 56:1952;514-523.
    • (1952) J. Phys. Chem. , vol.56 , pp. 514-523
    • Gralén, N.1    Lagermalm, G.2
  • 54
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre J., Huertas M.L., Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78:2000;719-730.
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia Dela Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 55
    • 0027330865 scopus 로고
    • Modeling the alpha IIb beta 3 integrin solution conformation
    • Rocco M., Spotorno B., Hantgan R.R. Modeling the alpha IIb beta 3 integrin solution conformation. Protein Sci. 2:1993;2154-2166.
    • (1993) Protein Sci. , vol.2 , pp. 2154-2166
    • Rocco, M.1    Spotorno, B.2    Hantgan, R.R.3
  • 56
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • Morgan P.J., Hyman S.C., Byron O., Andrew P.W., Mitchell T.J., Rowe A.J. Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J. Biol. Chem. 269:1994;25315-25320.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25315-25320
    • Morgan, P.J.1    Hyman, S.C.2    Byron, O.3    Andrew, P.W.4    Mitchell, T.J.5    Rowe, A.J.6
  • 57
    • 0033920488 scopus 로고    scopus 로고
    • Hydrodynamic bead modeling of biological macromolecules
    • Byron O. Hydrodynamic bead modeling of biological macromolecules. Methods Enzymol. 321:2000;278-304.
    • (2000) Methods Enzymol. , vol.321 , pp. 278-304
    • Byron, O.1
  • 59
    • 0000563335 scopus 로고
    • Effect of pressure on the viscosity of water
    • Bett K.E., Cappi J.B. Effect of pressure on the viscosity of water. Nature. 207:1965;620-621.
    • (1965) Nature , vol.207 , pp. 620-621
    • Bett, K.E.1    Cappi, J.B.2
  • 60
    • 1642266297 scopus 로고    scopus 로고
    • Pressure dependence of the viscosity of toluene
    • Kim J.R. Pressure dependence of the viscosity of toluene. J. Korean Chem. Soc. 43:1999;251-256.
    • (1999) J. Korean Chem. Soc. , vol.43 , pp. 251-256
    • Kim, J.R.1


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