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Volumn 77, Issue 6, 1999, Pages 2902-2910

Novel size-independent modeling of the dilute solution conformation of the immunoglobulin IgG Fab' domain using SOLPRO and ELLIPS

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYHEMOGLOBIN; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY B.72.3; RIBONUCLEASE;

EID: 0344339735     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77123-7     Document Type: Article
Times cited : (26)

References (53)
  • 1
    • 0028812441 scopus 로고
    • Structure of an antiidiotypic fab against feline peritoni virus-neutralizing antibody and a comparison with the complexed fab
    • Ban, N., C. Excobar, K. W. Hasel, J. Day, and A. Greenwood. 1995. Structure of an antiidiotypic fab against feline peritoni virus-neutralizing antibody and a comparison with the complexed Fab. FASEB J. 9:107-114.
    • (1995) FASEB J. , vol.9 , pp. 107-114
    • Ban, N.1    Excobar, C.2    Hasel, K.W.3    Day, J.4    Greenwood, A.5
  • 2
    • 0031253786 scopus 로고    scopus 로고
    • VL:VH domain rotations in engineered antibodies: Crystal structures of the Fab fragments from two murine anti-tumour antibodies and their engineered constructs
    • Banfield, M. J., D. J. King, A. Mountain, and R. K. Brady. 1997. VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine anti-tumour antibodies and their engineered constructs. Proteins Struct. Funct. Genet. 29:161-171.
    • (1997) Proteins Struct. Funct. Genet. , vol.29 , pp. 161-171
    • Banfield, M.J.1    King, D.J.2    Mountain, A.3    Brady, R.K.4
  • 3
    • 0031029481 scopus 로고    scopus 로고
    • Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
    • Behlke, J., and O. Ristau. 1997. Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72:428-434.
    • (1997) Biophys. J. , vol.72 , pp. 428-434
    • Behlke, J.1    Ristau, O.2
  • 4
    • 0015267987 scopus 로고
    • Der einfluss von sauerstoff auf die reversible spaltung des menschlichen desoxyhamoglobins im elektrolytarmen milieu
    • Behlke, J., and W. Scheler. 1972. Der einfluss von Sauerstoff auf die reversible Spaltung des menschlichen Desoxyhamoglobins im elektrolytarmen Milieu. Acta Biol. Med. Ger. 28:K1-K4.
    • (1972) Acta Biol. Med. Ger. , vol.28
    • Behlke, J.1    Scheler, W.2
  • 5
    • 0014057375 scopus 로고
    • Frictional coefficients of multisubunit structures
    • Bloomfield, V. A., W. O. Dalton, and K. E. van Holde. 1967. Frictional coefficients of multisubunit structures. Biopolymers. 5:135-148.
    • (1967) Biopolymers , vol.5 , pp. 135-148
    • Bloomfield, V.A.1    Dalton, W.O.2    Van Holde, K.E.3
  • 9
    • 0033039369 scopus 로고    scopus 로고
    • Hydrodynamic properties of rigid particles: Comparison of different modeling and computational procedures
    • Carrasco, B., and J. Garcia de la Torre. 1999. Hydrodynamic properties of rigid particles: comparison of different modeling and computational procedures. Biophys. J. 76:3044-3057.
    • (1999) Biophys. J. , vol.76 , pp. 3044-3057
    • Carrasco, B.1    Garcia De La Torre, J.2
  • 10
    • 0142229698 scopus 로고    scopus 로고
    • MSTARA and MSTARI: Interactive PC algorithms for simple, model independent evaluation of sedimentation equilibrium data
    • Cölfen, H., and S. E. Harding. 1997. MSTARA and MSTARI: interactive PC algorithms for simple, model independent evaluation of sedimentation equilibrium data. Eur. Biophys. J. 25:333-346.
    • (1997) Eur. Biophys. J. , vol.25 , pp. 333-346
    • Cölfen, H.1    Harding, S.E.2
  • 11
    • 0009722952 scopus 로고
    • Studies of free diffusion in liquids with the Rayleigh method. III. The analysis of known mixtures and some preliminary investigations with proteins
    • Creeth, J. M. 1958. Studies of free diffusion in liquids with the Rayleigh method. III. The analysis of known mixtures and some preliminary investigations with proteins. J. Phys. Chem. 62:66-74.
    • (1958) J. Phys. Chem. , vol.62 , pp. 66-74
    • Creeth, J.M.1
  • 12
    • 0020440294 scopus 로고
    • Some observations of a new type of point average molecular weight
    • Creeth, J. M., and S. E. Harding. 1982. Some observations of a new type of point average molecular weight. J. Biochem. Biophys. Methods. 7:25-34.
    • (1982) J. Biochem. Biophys. Methods , vol.7 , pp. 25-34
    • Creeth, J.M.1    Harding, S.E.2
  • 13
    • 0002872612 scopus 로고
    • Hydrodynamic properties of macromolecular assemblies
    • S. E. Harding and A. J. Rowe, editors. Royal Society of Chemistry, Cambridge, England
    • Garcia de la Torre, J. 1989. Hydrodynamic properties of macromolecular assemblies. In Dynamic Properties of Biomolecular Assemblies. S. E. Harding and A. J. Rowe, editors. Royal Society of Chemistry, Cambridge, England. 3-31.
    • (1989) Dynamic Properties of Biomolecular Assemblies , pp. 3-31
    • Garcia De La Torre, J.1
  • 14
    • 0017403408 scopus 로고
    • Hydrodynamic properties of macromolecular complexes
    • Garcia de la Torre, J., and V. A. Bloomfield. 1977. Hydrodynamic properties of macromolecular complexes. Biopolymers. 16:1747-1763.
    • (1977) Biopolymers , vol.16 , pp. 1747-1763
    • Garcia De La Torre, J.1    Bloomfield, V.A.2
  • 15
    • 0019526265 scopus 로고
    • Hydrodynamic properties of complex, rigid, biological macromolecules: Theory and applications
    • Garcia de la Torre, J., and V. A. Bloomfield. 1981. Hydrodynamic properties of complex, rigid, biological macromolecules: theory and applications. Q. Rev. Biophys. 14:81-139.
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 81-139
    • Garcia De La Torre, J.1    Bloomfield, V.A.2
  • 16
    • 0000203062 scopus 로고    scopus 로고
    • Intrinsic viscosity and rotational diffusion of bead models for rigid macromolecules and bioparticles
    • Garcia de la Torre, J., and B. Carrasco. 1998. Intrinsic viscosity and rotational diffusion of bead models for rigid macromolecules and bioparticles. Eur. Biophys. J. 27:549-557.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 549-557
    • Garcia De La Torre, J.1    Carrasco, B.2
  • 17
    • 0030793360 scopus 로고    scopus 로고
    • SOLPRO: Theory and computer program for the prediction of solution properties of rigid macromolecules and bioparticles
    • Garcia de la Torre, J., B. Carrasco, and S. E. Harding. 1997. SOLPRO: theory and computer program for the prediction of solution properties of rigid macromolecules and bioparticles. Eur. Biophys. J. 25:361-372.
    • (1997) Eur. Biophys. J. , vol.25 , pp. 361-372
    • Garcia De La Torre, J.1    Carrasco, B.2    Harding, S.E.3
  • 18
    • 0005777458 scopus 로고    scopus 로고
    • Calculation of NMR relaxation, covolume, and scattering-related properties of bead models using the SOL-PRO computer program
    • Garcia de la Torre, J., S. E. Harding, and B. Carrasco. 1999. Calculation of NMR relaxation, covolume, and scattering-related properties of bead models using the SOL-PRO computer program. Eur. Biophys. J. 28: 119-132.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 119-132
    • Garcia De La Torre, J.1    Harding, S.E.2    Carrasco, B.3
  • 19
    • 36749114754 scopus 로고
    • Effects from bead size and hydrodynamic interactions on the translational and rotational coefficients of macromolecular bead models
    • Garcia de la Torre, J., and V. Rodes. 1983. Effects from bead size and hydrodynamic interactions on the translational and rotational coefficients of macromolecular bead models. J. Chem. Phys. 79:2454-2460.
    • (1983) J. Chem. Phys. , vol.79 , pp. 2454-2460
    • Garcia De La Torre, J.1    Rodes, V.2
  • 20
    • 0008221693 scopus 로고
    • The optima XL-A: A new analytical ultracentrifuge with a novel precision absorption optical system
    • S. E. Harding, A. J. Rowe, and J. C. Horton, editors. Royal Society of Chemistry, Cambridge, England
    • Giebeler, R. 1992. The Optima XL-A: a new analytical ultracentrifuge with a novel precision absorption optical system. In Analytical Ultracentrifugation in Biochemistry and Polymer Science. S. E. Harding, A. J. Rowe, and J. C. Horton, editors. Royal Society of Chemistry, Cambridge, England.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science
    • Giebeler, R.1
  • 22
    • 33947343329 scopus 로고
    • The preparation of acetate and phosphate buffer solutions of known pH and ionic strength
    • Green, A. A. 1933. The preparation of acetate and phosphate buffer solutions of known pH and ionic strength. J. Am. Chem. Soc. 55: 2331-2336.
    • (1933) J. Am. Chem. Soc. , vol.55 , pp. 2331-2336
    • Green, A.A.1
  • 23
    • 0024581847 scopus 로고
    • A B72.3 second generation monoclonal antibody CC49 defines the mucin carried carbohydrate epitope Galβ(1-3)[NeuAcα(2-6)]GalNAc
    • Hanisch, F. G., G. Uhlenbruck, H. Egge, and J. Peter-Katalinic. 1989. A B72.3 second generation monoclonal antibody CC49 defines the mucin carried carbohydrate epitope Galβ(1-3)[NeuAcα(2-6)]GalNAc. Biol. Chem. Hoppe-Seyler. 370:21-26.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 21-26
    • Hanisch, F.G.1    Uhlenbruck, G.2    Egge, H.3    Peter-Katalinic, J.4
  • 24
    • 0002331258 scopus 로고
    • Modelling the gross conformation of assemblies using hydrodynamics: The whole body approach
    • S. E. Harding and A. J. Rowe, editors. Royal Society of Chemistry, Cambridge, England
    • Harding, S. E. 1989. Modelling the gross conformation of assemblies using hydrodynamics: the whole body approach. In Dynamic Properties of Biomolecular Assemblies. S. E. Harding and A. J. Rowe, editors. Royal Society of Chemistry, Cambridge, England. 32-56.
    • (1989) Dynamic Properties of Biomolecular Assemblies , pp. 32-56
    • Harding, S.E.1
  • 25
    • 0030793359 scopus 로고    scopus 로고
    • The ELLIPS suite of macromolecular conformation algorithms
    • Harding, S. E., J. C. Horton, and H. Cölfen. 1997 The ELLIPS suite of macromolecular conformation algorithms. Eur. Biophys. J. 25:347-359.
    • (1997) Eur. Biophys. J. , vol.25 , pp. 347-359
    • Harding, S.E.1    Horton, J.C.2    Cölfen, H.3
  • 26
    • 0033031360 scopus 로고    scopus 로고
    • COVOL: An interactive program for evaluating second virial coefficients from the triaxial shape or dimensions of rigid macromolecules
    • Harding, S. E., J. C. Horton, S. Jones, J. M. Thornton, and D. J. Winzor. 1999. COVOL: an interactive program for evaluating second virial coefficients from the triaxial shape or dimensions of rigid macromolecules. Biophys. J. 76:2432-2438.
    • (1999) Biophys. J. , vol.76 , pp. 2432-2438
    • Harding, S.E.1    Horton, J.C.2    Jones, S.3    Thornton, J.M.4    Winzor, D.J.5
  • 27
    • 0022351381 scopus 로고
    • The concentration dependence of macromolecular parameters
    • Harding, S. E., and P. Johnson. 1985a. The concentration dependence of macromolecular parameters. Biochem. J. 231:543-547.
    • (1985) Biochem. J. , vol.231 , pp. 543-547
    • Harding, S.E.1    Johnson, P.2
  • 28
    • 0022157026 scopus 로고
    • Physicochemical studies on turnip-yellow-mosaic virus
    • Harding, S. E., and P. Johnson. 1985b. Physicochemical studies on turnip-yellow-mosaic virus. Biochem. J. 231:549-555.
    • (1985) Biochem. J. , vol.231 , pp. 549-555
    • Harding, S.E.1    Johnson, P.2
  • 29
    • 0000505523 scopus 로고
    • Modelling biological macromolecules in solution. 1. The ellipsoid of revolution
    • Harding, S. E., and A. J. Rowe. 1982a. Modelling biological macromolecules in solution. 1. The ellipsoid of revolution. Int. J. Biol. Macromol. 4:160-164.
    • (1982) Int. J. Biol. Macromol. , vol.4 , pp. 160-164
    • Harding, S.E.1    Rowe, A.J.2
  • 30
    • 0010508023 scopus 로고
    • Modelling biological macromolecules in solution. 3. The L-R intersection method for triaxial ellipsoids
    • Harding, S. E., and A. J. Rowe. 1982b. Modelling biological macromolecules in solution. 3. The L-R intersection method for triaxial ellipsoids. Int. J. Biol. Macromol. 4:357-361.
    • (1982) Int. J. Biol. Macromol. , vol.4 , pp. 357-361
    • Harding, S.E.1    Rowe, A.J.2
  • 31
    • 0020794454 scopus 로고
    • Modelling biological macromolecules in solution. II. The general triaxial ellipsoid
    • Harding, S. E., and A. J. Rowe. 1983. Modelling biological macromolecules in solution. II. The general triaxial ellipsoid. Biopolymers. 22: 1813-1829 and 23:843.
    • (1983) Biopolymers , vol.22 , pp. 1813-1829
    • Harding, S.E.1    Rowe, A.J.2
  • 32
    • 0031844118 scopus 로고    scopus 로고
    • Comparison of the conformations of two monoclonal antibodies with hinges
    • Harris, L. J., S. B. Larson, E. Skaletsky, and A. McPherson. 1998a. Comparison of the conformations of two monoclonal antibodies with hinges. Immunol. Rev. 163:35-43.
    • (1998) Immunol. Rev. , vol.163 , pp. 35-43
    • Harris, L.J.1    Larson, S.B.2    Skaletsky, E.3    McPherson, A.4
  • 33
    • 0032488888 scopus 로고    scopus 로고
    • Crystallographic structure of an intact IgG1 monoclonal antibody
    • Harris, L. J., E. Skaletsky, and E. McPherson. 1998b. Crystallographic structure of an intact IgG1 monoclonal antibody. J. Mol. Biol. 275: 861-872.
    • (1998) J. Mol. Biol. , vol.275 , pp. 861-872
    • Harris, L.J.1    Skaletsky, E.2    McPherson, E.3
  • 35
  • 36
    • 0020209703 scopus 로고
    • Estimation of sedimentation coefficients of globular proteins: An application of small-angle x-ray scattering
    • Kumoninski, T. F., and H. Pessen. 1982. Estimation of sedimentation coefficients of globular proteins: an application of small-angle x-ray scattering. Arch. Biochem. Biophys. 219:89-100.
    • (1982) Arch. Biochem. Biophys. , vol.219 , pp. 89-100
    • Kumoninski, T.F.1    Pessen, H.2
  • 37
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski, R. A. 1995. SURFNET: a program for visualizing molecular surfaces, cavities and intermolecular interactions. J. Mol. Graph. 13: 323-330.
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 39
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. 1986. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:169-180.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 40
    • 0000856458 scopus 로고
    • Mouvement Brownian d'un ellipsoide. I. Dispersion dielectrique pour des molecules ellipsoidales
    • Perrin, F. 1934. Mouvement Brownian d'un ellipsoide. I. Dispersion dielectrique pour des molecules ellipsoidales. J. Phys. Radium. 5:497-511.
    • (1934) J. Phys. Radium. , vol.5 , pp. 497-511
    • Perrin, F.1
  • 41
    • 0002821446 scopus 로고
    • Mouvement Brownian d'un ellipsoide. II. Rotation libre et depolarisation des fluorescences. Translation et diffusion de molecules ellipsoidales
    • Perrin, F. 1936. Mouvement Brownian d'un ellipsoide. II. Rotation libre et depolarisation des fluorescences. Translation et diffusion de molecules ellipsoidales. J. Phys. Radium. 7:1-11.
    • (1936) J. Phys. Radium. , vol.7 , pp. 1-11
    • Perrin, F.1
  • 42
    • 0015091666 scopus 로고
    • The use of small-angle x-ray scattering to determine protein conformation
    • Pessen, H., T. F. Kumoninski, and S. N. Timasheff. 1971. The use of small-angle x-ray scattering to determine protein conformation. J. Agric. Food Chem. 19:698-702.
    • (1971) J. Agric. Food Chem. , vol.19 , pp. 698-702
    • Pessen, H.1    Kumoninski, T.F.2    Timasheff, S.N.3
  • 43
    • 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
  • 44
    • 0026706824 scopus 로고
    • Crystal structure of human-immunoglobulin fragment refined at 2.0-Angstrom resolution
    • Saul, F. A., and R. J. Poljak. 1992. Crystal structure of human-immunoglobulin fragment refined at 2.0-Angstrom resolution. Proteins Struct. Fund. Genet. 14:363-371.
    • (1992) Proteins Struct. Fund. Genet. , vol.14 , pp. 363-371
    • Saul, F.A.1    Poljak, R.J.2
  • 46
    • 0002276429 scopus 로고
    • The influence of Brownian motion on the viscosity of solutions
    • Simha, R. 1940. The influence of Brownian motion on the viscosity of solutions. J. Phys. Chem, 44:25-34.
    • (1940) J. Phys. Chem , vol.44 , pp. 25-34
    • Simha, R.1
  • 47
  • 48
    • 0002114003 scopus 로고
    • Methods for obtaining sedimentation coefficient distributions
    • S. E. Harding, A. J. Rowe, and J. C. Horton, editors. Royal Society of Chemistry, Cambridge, England
    • Stafford, W. F. 1992. Methods for obtaining sedimentation coefficient distributions. In Analytical Ultracentrifugation in Biochemistry and Polymer Science. S. E. Harding, A. J. Rowe, and J. C. Horton, editors. Royal Society of Chemistry, Cambridge, England. 359-393.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 359-393
    • Stafford, W.F.1
  • 52
  • 53
    • 0028867347 scopus 로고
    • Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins
    • Zhou, H.-X. 1995. Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins. Biophys. J. 69:2298-2303.
    • (1995) Biophys. J. , vol.69 , pp. 2298-2303
    • Zhou, H.-X.1


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