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Direct analysis of sedimentation equilibrium distributions reflecting macromolecular interactions

  • P. R. Wills
  • M. P. Jacobsen
  • D. J. WinzorEmail author
Keynote Lectures
Part of the Progress in Colloid & Polymer Science book series (PROGCOLLOID, volume 107)

Abstract

This review of the characterization of protein interactions by sedimentation equilibrium emphasizes procedures that entail direct determination of the thermodynamic activity of the smallest species contributing to the concentration distribution for that constituent. This approach, which has been regarded as an Australasian oddity for over two decades, is first illustrated by evaluating the association constant for α-chymotrypsin dimerization by the original omega analysis and subsequent refinements thereof. Notable in that regard is the introduction of the psi function, which has evolved from its omega counterpart. Application of the corresponding approach to sedimentation distributions for mixtures of ovalbumin and cytochrome c is presented to illustrate the potential of the psi function for characterizing interactions between dissimilar macromolecular reactants. Also discussed is the means by which these direct analyses of sedimentation equilibrium distributions afford realistic allowance for effects of thermodynamic nonideality on the statistical-mechanical basis of excluded volume.

Key words

Protein self-association heterogeneous association sedimentation equilibrium thermodynamic nonideality 

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Copyright information

© Dr. Dietrich Steinkopff Verlag GmbH & Co. KG 1997

Authors and Affiliations

  1. 1.Department of PhysicsUniversity of AucklandAucklandNew Zealand
  2. 2.Centre for Protein Structure, Function and Engineering Department of BiochemistryUniversity of QueenslandBrisbaneAustralia

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