Investigation of antibody structures by scattering techniques

L. Cser, I. A. Gladkib, F. Franek, Yu M. Ostanevich

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Different experimental methods - hydrodynamical measurements, electronmicroscopy, X-ray crystallography, Yray and neutron small-angle scattering - provide data on the shape and dimensions of immunoglobulin molecules. Comparison of these data using model computation shows that the shape of IgG immunoglobulin in dissolved state differs from that in crystalline state. The same statement is valid for the shape of Fab and Fc fragments. Immunoglobulins of different origin have different dimensions. Correlation between the number of interchain disulphide bonds and the values of the radius of gyration may be observed. The value of the radius of gyration decreases when the IgG molecule binds haptens while the shape of the molecule seems to remain unchanged. This effect has a nonlinear dependence on the saturation of binding sites and may be connected with the effector function of IgG molecule.

Original languageEnglish
Pages (from-to)625-640
Number of pages16
JournalColloid and Polymer Science Kolloid Zeitschrift & Zeitschrift für Polymere
Volume259
Issue number6
DOIs
Publication statusPublished - Jun 1 1981

Keywords

  • Immunglobulin
  • X-ray
  • conformation
  • contrast variation
  • electronmicroscopy
  • model computation
  • neutron scattering

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Polymers and Plastics
  • Colloid and Surface Chemistry
  • Materials Chemistry

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