메뉴 건너뛰기




Volumn 178, Issue 2, 2008, Pages 105-120

A new adaptive grid-size algorithm for the simulation of sedimentation velocity profiles in analytical ultracentrifugation

Author keywords

Analytical ultracentrifugation; Finite element methods; Protein interactions; Size distributions

Indexed keywords

ALGORITHMS; CENTRIFUGATION; FINITE ELEMENT METHOD; PROTEINS; SIZE DISTRIBUTION;

EID: 37249086336     PISSN: 00104655     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cpc.2007.08.012     Document Type: Article
Times cited : (80)

References (78)
  • 2
    • 0001479980 scopus 로고
    • A new method for the determination of the molecular weight of the proteins
    • Svedberg T., and Fahraeus R. A new method for the determination of the molecular weight of the proteins. J. Am. Chem. Soc. 48 (1926) 320-438
    • (1926) J. Am. Chem. Soc. , vol.48 , pp. 320-438
    • Svedberg, T.1    Fahraeus, R.2
  • 4
    • 84982335864 scopus 로고
    • Ultrazentrifugale Polydispersitätsbestimmungen an hochpolymeren Stoffen
    • Signer R., and 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
  • 6
    • 0008531095 scopus 로고
    • Reversible association processes of globular proteins. V. The study of associating systems by the methods of macromolecular physics
    • Steiner R.F. Reversible association processes of globular proteins. V. The study of associating systems by the methods of macromolecular physics. Arch. Biochem. Biophys. 49 (1954) 400-416
    • (1954) Arch. Biochem. Biophys. , vol.49 , pp. 400-416
    • Steiner, R.F.1
  • 7
    • 0032964389 scopus 로고    scopus 로고
    • Characterizing the solution properties of supramolecular systems by analytical ultracentrifugation
    • Schubert D., Tziatzios C., Schuck P., and 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
  • 8
    • 0035532303 scopus 로고    scopus 로고
    • Molecular and structural characteristics of lactodendrimers based on poly(amidoamine)
    • Pavlov G.M., Errington N., Harding S.E., Korneeva E.V., and Roy R. Molecular and structural characteristics of lactodendrimers based on poly(amidoamine). Polymer Sci. Ser. A 43 (2001) 118-123
    • (2001) Polymer Sci. Ser. A , vol.43 , pp. 118-123
    • Pavlov, G.M.1    Errington, N.2    Harding, S.E.3    Korneeva, E.V.4    Roy, R.5
  • 9
    • 33646149783 scopus 로고    scopus 로고
    • Synthesis of an anionically chargeable, high-molar-mass, second-generation dendronized polymer and the observation of branching by scanning force microscopy
    • Kasemi E., Zhuang W., Rabe J.P., Fischer K., Schmidt M., Colussi M., Keul H., Yi D., Colfen H., and Schluter A.D. Synthesis of an anionically chargeable, high-molar-mass, second-generation dendronized polymer and the observation of branching by scanning force microscopy. J. Am. Chem. Soc. 128 (2006) 5091-5099
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5091-5099
    • Kasemi, E.1    Zhuang, W.2    Rabe, J.P.3    Fischer, K.4    Schmidt, M.5    Colussi, M.6    Keul, H.7    Yi, D.8    Colfen, H.9    Schluter, A.D.10
  • 10
    • 84986754612 scopus 로고
    • Modern methods for determining the molar mass distribution of polymers. General considerations and application to sedimentation equilibrium
    • Lechner M.D., and Mächtle W. Modern methods for determining the molar mass distribution of polymers. General considerations and application to sedimentation equilibrium. Makromol. Chem., Makromol. Symp. 61 (1992) 165-175
    • (1992) Makromol. Chem., Makromol. Symp. , vol.61 , pp. 165-175
    • Lechner, M.D.1    Mächtle, W.2
  • 13
    • 37249084453 scopus 로고    scopus 로고
    • Monitoring the homogeneity of adenovirus preparations (a gene therapy delivery system) using analytical ultracentrifugation
    • Berkowitz S.A., and Philo J.S. Monitoring the homogeneity of adenovirus preparations (a gene therapy delivery system) using analytical ultracentrifugation. Anal. Biochem. (2006)
    • (2006) Anal. Biochem.
    • Berkowitz, S.A.1    Philo, J.S.2
  • 14
    • 33749506729 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of amyloid oligomers and fibrils
    • Mok Y.F., and Howlett G.J. Sedimentation velocity analysis of amyloid oligomers and fibrils. Methods Enzymol. 413 (2006) 199-217
    • (2006) Methods Enzymol. , vol.413 , pp. 199-217
    • Mok, Y.F.1    Howlett, G.J.2
  • 15
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire S.J., Shahrokh Z., and Liu J. Challenges in the development of high protein concentration formulations. J. Pharmaceutical Sci. 93 (2004) 1390-1402
    • (2004) J. Pharmaceutical Sci. , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 16
    • 33749452453 scopus 로고    scopus 로고
    • A critical review of analytical ultracentrifugation and field flow fractionation methods for measuring protein aggregation
    • Liu J., Andya J.D., and Shire S.J. A critical review of analytical ultracentrifugation and field flow fractionation methods for measuring protein aggregation. Aaps J. 8 (2006) E580-E589
    • (2006) Aaps J. , vol.8
    • Liu, J.1    Andya, J.D.2    Shire, S.J.3
  • 17
    • 33749372201 scopus 로고    scopus 로고
    • Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals
    • Berkowitz S.A. Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals. Aaps J. 8 (2006) E590-E605
    • (2006) Aaps J. , vol.8
    • Berkowitz, S.A.1
  • 18
    • 33847683955 scopus 로고    scopus 로고
    • Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity
    • Gabrielson J.P., Brader M.L., Pekar A.H., Mathis K.B., Winter G., Carpenter J.F., and Randolph T.W. Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity. J. Pharm. Sci. 96 (2006) 268-279
    • (2006) J. Pharm. Sci. , vol.96 , pp. 268-279
    • Gabrielson, J.P.1    Brader, M.L.2    Pekar, A.H.3    Mathis, K.B.4    Winter, G.5    Carpenter, J.F.6    Randolph, T.W.7
  • 19
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: a tutorial review
    • Lebowitz J., Lewis M.S., and 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
  • 20
    • 33644491645 scopus 로고    scopus 로고
    • Golemis E., and Adams P.D. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Balbo A., and Schuck P. In: Golemis E., and Adams P.D. (Eds). Protein-Protein Interactions (2005), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York 253-277
    • (2005) Protein-Protein Interactions , pp. 253-277
    • Balbo, A.1    Schuck, P.2
  • 21
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • Howlett G.J., Minton A.P., and Rivas G. 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
  • 24
    • 0003159229 scopus 로고
    • Die Differentialgleichung der Ultrazentrifugierung
    • Lamm O. Die Differentialgleichung der Ultrazentrifugierung. Ark. Mat. Astr. Fys. 21B 2 (1929) 1-4
    • (1929) Ark. Mat. Astr. Fys. , vol.21 B , Issue.2 , pp. 1-4
    • Lamm, O.1
  • 25
    • 33947462968 scopus 로고
    • A demonstration of some new methods of determining molecular weights from the data of the ultracentrifuge
    • Archibald W.J. A demonstration of some new methods of determining molecular weights from the data of the ultracentrifuge. J. Phys. & Colloid. Chem. 51 (1947) 1204-1214
    • (1947) J. Phys. & Colloid. Chem. , vol.51 , pp. 1204-1214
    • Archibald, W.J.1
  • 26
    • 0342912457 scopus 로고
    • Über eine Differentialgleichung aus der physikalischen Chemie
    • Faxén H. Über eine Differentialgleichung aus der physikalischen Chemie. Ark. Mat. Astr. Fys. 21B (1929) 1-6
    • (1929) Ark. Mat. Astr. Fys. , vol.21 B , pp. 1-6
    • Faxén, H.1
  • 27
    • 0342912456 scopus 로고
    • Extension of sedimentation velocity theory to molecules of intermediate sizes
    • Fujita H., and MacCosham V.J. Extension of sedimentation velocity theory to molecules of intermediate sizes. J. Chem. Phys. 30 (1959) 291-298
    • (1959) J. Chem. Phys. , vol.30 , pp. 291-298
    • Fujita, H.1    MacCosham, V.J.2
  • 30
    • 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
  • 31
    • 84984088128 scopus 로고
    • Numerical simulations of the Lamm equation: III. Velocity centrifugation
    • Dishon M., Weiss G.H., and Yphantis D.A. Numerical simulations of the Lamm equation: III. Velocity centrifugation. Biopolymers 5 (1967) 697-713
    • (1967) Biopolymers , vol.5 , pp. 697-713
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 32
    • 1642326461 scopus 로고
    • Numerical solutions of the Lamm equation. VI. Effects of hydrostatic pressure on velocity sedimentation of two-component systems
    • Dishon M., Weiss G.H., and Yphantis D.A. Numerical solutions of the Lamm equation. VI. Effects of hydrostatic pressure on velocity sedimentation of two-component systems. J. Polym. Sci. 8 (1970) 2163-2175
    • (1970) J. Polym. Sci. , vol.8 , pp. 2163-2175
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 33
    • 0342822263 scopus 로고
    • Kinetics of sedimentation in a density gradient
    • Dishon M., Weiss G.H., and Yphantis D.A. Kinetics of sedimentation in a density gradient. Biopolymers 10 (1971) 2095-2111
    • (1971) Biopolymers , vol.10 , pp. 2095-2111
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 34
    • 0014439427 scopus 로고
    • Computer simulation of sedimentation in the ultracentrifuge. IV. Velocity sedimentation of self-associating solutes
    • Cox D.J. Computer simulation of sedimentation in the ultracentrifuge. IV. Velocity sedimentation of self-associating solutes. Arch. Biochem. Biophys. 129 (1969) 106-123
    • (1969) Arch. Biochem. Biophys. , vol.129 , pp. 106-123
    • Cox, D.J.1
  • 35
    • 84981860451 scopus 로고
    • Theory of sedimentation of interacting systems
    • Goad W.B., and Cann J.R. Theory of sedimentation of interacting systems. Ann. NY Acad. Sci. 164 (1969) 172-182
    • (1969) Ann. NY Acad. Sci. , vol.164 , pp. 172-182
    • Goad, W.B.1    Cann, J.R.2
  • 37
    • 0016753958 scopus 로고
    • Sedimentation of generalized systems of interacting particles. II. Active enzyme centrifugation-theory and extensions of its validity range
    • Cohen R., and Claverie J.M. Sedimentation of generalized systems of interacting particles. II. Active enzyme centrifugation-theory and extensions of its validity range. Biopolymers 14 (1975) 1701-1716
    • (1975) Biopolymers , vol.14 , pp. 1701-1716
    • Cohen, R.1    Claverie, J.M.2
  • 38
    • 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
  • 39
    • 0031029481 scopus 로고    scopus 로고
    • Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
    • Behlke J., and Ristau O. Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72 (1997) 428-434
    • (1997) Biophys. J. , vol.72 , pp. 428-434
    • Behlke, J.1    Ristau, O.2
  • 40
    • 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., and 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
  • 41
    • 0031962095 scopus 로고    scopus 로고
    • Determination of sedimentation coefficients for small peptides
    • Schuck P., MacPhee C.E., and 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
  • 42
    • 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
  • 43
    • 24144485161 scopus 로고    scopus 로고
    • Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution of the Lamm equation
    • Cao W., and Demeler B. Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution of the Lamm equation. Biophys. J. 89 (2005) 1589-1602
    • (2005) Biophys. J. , vol.89 , pp. 1589-1602
    • Cao, W.1    Demeler, B.2
  • 44
    • 37249073180 scopus 로고    scopus 로고
    • B. Kindler, PhD Thesis, University Hannover, Hannover, Germany, 1997
  • 45
    • 0011203173 scopus 로고
    • Complete evaluation of sedimentation velocity experiments in the analytical ultracentrifuge
    • Urbanke C., Ziegler B., and Stieglitz K. Complete evaluation of sedimentation velocity experiments in the analytical ultracentrifuge. Fresenius Z. Anal. Chem. 301 (1980) 139-140
    • (1980) Fresenius Z. Anal. Chem. , vol.301 , pp. 139-140
    • Urbanke, C.1    Ziegler, B.2    Stieglitz, K.3
  • 46
    • 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
    • Stafford W.F., and Sherwood P.J. 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
  • 47
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • Demeler B., Saber H., and 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
  • 48
    • 37249092302 scopus 로고    scopus 로고
    • Schuck P. (2007). www.analyticalultracentrifugation.com
    • (2007)
    • Schuck, P.1
  • 49
    • 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
  • 50
    • 37249040782 scopus 로고    scopus 로고
    • Schuck P. (2007). www.analyticalultracentrifugation.com/sedphat/sedphat.htm
    • (2007)
    • Schuck, P.1
  • 51
    • 0033058274 scopus 로고    scopus 로고
    • Direct sedimentation analysis of interference optical data in analytical ultracentrifugation
    • Schuck P., and 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
  • 52
    • 37249081856 scopus 로고    scopus 로고
    • Schuck P. (2007). http://www.analyticalultracentrifugation.com/references.htm
    • (2007)
    • Schuck, P.1
  • 53
    • 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
  • 54
    • 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., and 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
  • 55
    • 1842428822 scopus 로고    scopus 로고
    • Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity profiles
    • Dam J., and Schuck P. Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity profiles. Methods Enzymol. 384 (2004) 185-212
    • (2004) Methods Enzymol. , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 56
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown P.H., and Schuck P. Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys. J. 90 (2006) 4651-4661
    • (2006) Biophys. J. , vol.90 , pp. 4651-4661
    • Brown, P.H.1    Schuck, P.2
  • 58
    • 1642293193 scopus 로고    scopus 로고
    • A model for sedimentation in inhomogeneous media. I. Dynamic density gradients from sedimenting co-solutes
    • Schuck P. A model for sedimentation in inhomogeneous 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
  • 59
    • 20444380585 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c (s)
    • Dam J., Velikovsky C.A., Mariuzza R., Urbanke C., and Schuck P. 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
  • 60
    • 0032441422 scopus 로고    scopus 로고
    • Analytical band centrifugation of proteins and protein complexes
    • Lebowitz J., Teale M., and Schuck P. Analytical band centrifugation of proteins and protein complexes. Biochem. Soc. Transact. 26 (1998) 745-749
    • (1998) Biochem. Soc. Transact. , vol.26 , pp. 745-749
    • Lebowitz, J.1    Teale, M.2    Schuck, P.3
  • 61
    • 1642364826 scopus 로고    scopus 로고
    • A model for sedimentation in inhomogeneous media. II. Compressibility of aqueous and organic solvens
    • Schuck P. A model for sedimentation in inhomogeneous media. II. Compressibility of aqueous and organic solvens. Biophys. Chem. 187 (2004) 201-214
    • (2004) Biophys. Chem. , vol.187 , pp. 201-214
    • Schuck, P.1
  • 62
    • 0035971072 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes
    • Schuck P., Taraporewala Z., McPhie P., and Patton J.T. Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes. J. Biol. Chem. 276 (2000) 9679-9687
    • (2000) J. Biol. Chem. , vol.276 , pp. 9679-9687
    • Schuck, P.1    Taraporewala, Z.2    McPhie, P.3    Patton, J.T.4
  • 63
    • 0026544299 scopus 로고
    • Simulation of the time course of macromolecular separations in an ultracentrifuge. I. Formation of a cesium chloride density gradient at 25 °C
    • Minton A.P. Simulation of the time course of macromolecular separations in an ultracentrifuge. I. Formation of a cesium chloride density gradient at 25 °C. Biophys. Chem. 42 (1992) 13-21
    • (1992) Biophys. Chem. , vol.42 , pp. 13-21
    • Minton, A.P.1
  • 65
    • 0038365809 scopus 로고
    • Calculation of simulated sedimentation velocity profiles for self-associating solutes
    • Cox D.J. Calculation of simulated sedimentation velocity profiles for self-associating solutes. Methods Enzymol. 48 (1978) 212-231
    • (1978) Methods Enzymol. , vol.48 , pp. 212-231
    • Cox, D.J.1
  • 66
    • 37249044502 scopus 로고    scopus 로고
    • Schuck P. (2007). http://www.analyticalultracentrifugation.com/LammEqSolutions.htm
    • (2007)
    • Schuck, P.1
  • 67
    • 84984086797 scopus 로고
    • Numerical solutions of the Lamm equation. I. Numerical procedure
    • Dishon M., Weiss G.H., and Yphantis D.A. Numerical solutions of the Lamm equation. I. Numerical procedure. Biopolymers 4 (1966) 449-455
    • (1966) Biopolymers , vol.4 , pp. 449-455
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 68
    • 0016702458 scopus 로고
    • Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations
    • Claverie J.-M., Dreux H., and 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
  • 69
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck P., and 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
  • 70
    • 84953600891 scopus 로고
    • A practical method for numerical evaluation of solutions of partial differential equations of the heat-conduction type
    • Crank J., and Nicholson P. A practical method for numerical evaluation of solutions of partial differential equations of the heat-conduction type. Proc. Cambridge Philos. Soc. 43 (1947) 50-67
    • (1947) Proc. Cambridge Philos. Soc. , vol.43 , pp. 50-67
    • Crank, J.1    Nicholson, P.2
  • 71
    • 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
    • Dam J., and Schuck P. Sedimentation velocity analysis of protein-protein interactions: Sedimentation coefficient distributions c (s) and asymptotic boundary profiles from Gilbert-Jenkins theory. Biophys. J. 89 (2005) 651-666
    • (2005) Biophys. J. , vol.89 , pp. 651-666
    • Dam, J.1    Schuck, P.2
  • 72
    • 23344448481 scopus 로고    scopus 로고
    • A mechanism for assembly of complexes of vitronectin and plasminogen activator inhibitor-1 from sedimentation velocity analysis
    • Minor K.H., Schar C.R., Blouse G.E., Shore J.D., Lawrence D.A., Schuck P., and Peterson C.B. A mechanism for assembly of complexes of vitronectin and plasminogen activator inhibitor-1 from sedimentation velocity analysis. J. Biol. Chem. 31 (2005) 28711-28720
    • (2005) J. Biol. Chem. , vol.31 , pp. 28711-28720
    • Minor, K.H.1    Schar, C.R.2    Blouse, G.E.3    Shore, J.D.4    Lawrence, D.A.5    Schuck, P.6    Peterson, C.B.7
  • 74
    • 34247170432 scopus 로고    scopus 로고
    • Crystal structure of the Tp34 (TP0971) lipoprotein of treponema palladium: Implications of its metal-bound state and affinity for human lactoferrin
    • M610215200
    • Deka R.K., Brautigam C.A., Tomson F.L., Lumpkins S.B., Tomchick D.R., Machius M., and Norgard M.V. Crystal structure of the Tp34 (TP0971) lipoprotein of treponema palladium: Implications of its metal-bound state and affinity for human lactoferrin. J. Biol. Chem. Epub. (2007) M610215200
    • (2007) J. Biol. Chem. Epub.
    • Deka, R.K.1    Brautigam, C.A.2    Tomson, F.L.3    Lumpkins, S.B.4    Tomchick, D.R.5    Machius, M.6    Norgard, M.V.7
  • 75
    • 0014667373 scopus 로고
    • V. Chemically interacting systems. I. Theory of sedimentation of interacting systems
    • Goad W.B., and Cann J.R. V. Chemically interacting systems. I. Theory of sedimentation of interacting systems. Ann. NY Acad. Sci. 164 (1969) 192-225
    • (1969) Ann. NY Acad. Sci. , vol.164 , pp. 192-225
    • Goad, W.B.1    Cann, J.R.2
  • 76
    • 0017179272 scopus 로고
    • Sedimentation of generalized systems of interacting particles. III. Concentration-dependent sedimentation and extension to other transport methods
    • Claverie J.-M. Sedimentation of generalized systems of interacting particles. III. Concentration-dependent sedimentation and extension to other transport methods. Biopolymers 15 (1976) 843-857
    • (1976) Biopolymers , vol.15 , pp. 843-857
    • Claverie, J.-M.1
  • 77
    • 3042855150 scopus 로고    scopus 로고
    • The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O
    • Solovyova A.S., Nollmann M., Mitchell T.J., and Byron O. The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O. Biophys. J. 87 (2004) 540-552
    • (2004) Biophys. J. , vol.87 , pp. 540-552
    • Solovyova, A.S.1    Nollmann, M.2    Mitchell, T.J.3    Byron, O.4
  • 78
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: an immunological perspective
    • Rosenberg A.S. Effects of protein aggregates: an immunological perspective. Aaps J. 8 (2006) E501-E507
    • (2006) Aaps J. , vol.8
    • Rosenberg, A.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.