Computer Simulation of the Sedimentation of Ligand-Mediated and Kinetically Controlled Macromolecular Interactions

  • John R. Cann
Part of the Emerging Biochemical and Biophysical Techniques book series (EBBT)


Ultracentrifugal characterization of macromolecular interactions was initiated shortly after construction of the first analytical ultracentrifuge by Svedberg and his co-workers in 1925-26. Thus, following the immediate demonstration that proteins are distinct molecular entities with well defined mass and shape, not ill defined colloids, Svedberg (Svedberg and Pedersen, 1940) anticipated modern concepts of the subunit structure of proteins. Additionally, the prophetic studies on ligand-mediated association-dissociation of hemocyanins (Marimoto and Kegeles, 1971; Kegeles and Cann, 1978; Roxby et al. 1974; Miller and Van Holde, 1974) were initiated (Svedberg and Pedersen, 1940). Self-association of proteins and their interactions with each other and with low molecular weight ligands are central to current biological thought especially as they pertain to the mechanism of regulatory processes. Over the years one seminal finding for the development of biochemistry and molecular biology followed another. Early on, Heidelberger and Pedersen (1937) demonstrated the existence of soluble, protein antigen-antibody complexes in the antigen excess zone of the precipitin reaction. Subsequent ultracentrifuge studies of the soluble complexes by Singer et al. (Singer, 1965) provided direct confirmation of the framework theory of antigen- antibody precipitate and led, in conjunction with electrophoretic analysis, to thermodynamic characterization of antigen- antibody reactions via application of the Goldberg theory (Goldberg, 1952).


Sedimentation Velocity Sedimentation Pattern Sedimentation Coefficient Sedimentation Behavior Reaction Boundary 


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© Birkhäuser Boston 1994

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  • John R. Cann

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