Chapter title |
Sedimentation Equilibrium Studies
|
---|---|
Chapter number | 12 |
Book title |
Protein-Protein Interactions
|
Published in |
Methods in molecular biology, January 2015
|
DOI | 10.1007/978-1-4939-2425-7_12 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2424-0, 978-1-4939-2425-7
|
Authors |
Ian A. Taylor, Katrin Rittinger, John F. Eccleston, Taylor, Ian A., Rittinger, Katrin, Eccleston, John F. |
Abstract |
The reversible formation of protein-protein interactions plays a crucial role in many biological processes. In order to carry out a thorough quantitative characterization of these interactions it is essential to establish the oligomerization state of the individual components first. The sedimentation equilibrium method is ideally suited to perform these studies because it allows a reliable, accurate, and absolute value of the solution molecular weight of a macromolecule to be obtained. This technique is independent of the shape of the macromolecule under investigation and allows the determination of equilibrium constants for a monomer-multimer self-associating system. |
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