Abstract
The measurement and analysis of sedimentation equilibrium provides one of the most powerful and widely applicable methods for the characterization of reversible associations of macromolecules in solution. Recent developments in instrumentation, experimental design, and data analysis have substantially broadened the range of systems to which this technique may be applied, simplified its application, and reduced the cost of acquiring analytical capability.
Similar content being viewed by others
Article PDF
Author information
Authors and Affiliations
Rights and permissions
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/
About this article
Cite this article
Minton, A. Quantitative characterization of reversible macromolecular associations via sedimentation equilibrium: an introduction. Exp Mol Med 32, 1–5 (2000). https://doi.org/10.1038/emm.2000.1
Published:
Issue Date:
DOI: https://doi.org/10.1038/emm.2000.1
Keywords
This article is cited by
-
Protein–protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches
Cellular and Molecular Life Sciences (2014)
-
A High-Throughput Method for Detection of Protein Self-Association and Second Virial Coefficient Using Size-Exclusion Chromatography Through Simultaneous Measurement of Concentration and Scattered Light Intensity
Pharmaceutical Research (2007)