Measuring protein-protein interactions by equilibrium sedimentation

This unit describes basic principles and practice of sedimentation equilibrium analytical ultracentrifugation for the study of reversible protein interactions, such as the characterization of self-association, heterogeneous association, and binding stoichiometry, as well as the determination of asso...

Full description

Saved in:
Bibliographic Details
Published inCurrent protocols in immunology Vol. Chapter 18; p. 18.8.1
Main Authors Balbo, Andrea, Brown, Patrick H, Braswell, Emory H, Schuck, Peter
Format Journal Article
LanguageEnglish
Published United States 01.11.2007
Subjects
Animals
Chemistry Techniques, Analytical - instrumentation
Chemistry Techniques, Analytical - methods
Humans
Macromolecular Substances - isolation & purification
Macromolecular Substances - metabolism
Models, Theoretical
Protein Binding
Research Design
Software
Statistics as Topic - methods
Thermodynamics
Ultracentrifugation - instrumentation
Ultracentrifugation - methods
Online AccessGet more information

Cover

More Information
Summary:This unit describes basic principles and practice of sedimentation equilibrium analytical ultracentrifugation for the study of reversible protein interactions, such as the characterization of self-association, heterogeneous association, and binding stoichiometry, as well as the determination of association constants. Advanced tools such as mass conservation analysis, multiwavelength analysis, and global analysis are introduced and discussed in the context of the experimental design. A detailed protocol guiding the investigator through the experimental steps and the data analysis is available as an internet resource.
ISSN:1934-368X
DOI:10.1002/0471142735.im1808s79