UNIT 18.8 Measuring Protein-Protein Interactions by Equilibrium Sedimentation

  1. Peter Schuck1,
  2. Emory H. Braswell2

Published Online: 1 MAY 2001

DOI: 10.1002/0471142735.im1808s40

Current Protocols in Immunology

Current Protocols in Immunology

How to Cite

Schuck, P. and Braswell, E. H. 2001. Measuring Protein-Protein Interactions by Equilibrium Sedimentation. Current Protocols in Immunology. 18:18.8.

Author Information

  1. 1

    Molecular Interactions Resource, ORS, National Institutes of Health, Bethesda, Maryland

  2. 2

    National Analytical Ultracentrifugation Facility, University of Connecticut, Storrs, Connecticut

Publication History

  1. Published Online: 1 MAY 2001
  2. Published Print: DEC 2000

This is not the most recent version of the article. View current version (1 NOV 2007)


This commentary unit provides a basic introduction to the principles and practice of sedimentaiton equilibrium analytical ultracentrifugation for the study of reversible protein interactions. Equilibrium sedimentation is one of the most effective methods for the detection and characterization of protein interactions and can be applied to the measurement of self association, heterologous association, binding stoichiometry, and the determination of association constants. The unit includes an extensive discussion of the instrumentation required to carry out equilibrium analytical ultracentrifugation and to perform data analysis. A strategic planning section gives the reader several experimental scenarios and conditions for using equilibrium sedimentation.