Analytical ultracentrifugation for the study of protein association and assembly

Analytical ultracentrifugation for the study of protein association and assembly
Available online 28 August 2006.
Geoffrey J Howlett1, Allen P Minton2 and Germ?n Rivas3
Current Opinion in Chemical Biology
Volume 10, Issue 5 , October 2006
Copyright ? 2006 Elsevier Ltd All rights reserved.
1Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia
2Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda MD 20892-0830, USA
3Centro de Investigaciones Biol?gicas, CSIC, Ramiro de Maeztu 9, 28040-Madrid, Spain
Analytical ultracentrifugation remains pre-eminent among the methods used to study the interactions of macromolecules under physiological conditions. Recent developments in analytical procedures allow the high resolving power of sedimentation velocity methods to be coupled to sedimentation equilibrium approaches and applied to both static and dynamic associations. Improvements in global modeling based on numerical solutions of the Lamm equation have generated new sedimentation velocity applications with an emphasis on data interpretation using sedimentation coefficient or molar mass distributions. Procedures based on the use of multiple optical signals from absorption and interference optics for the analysis of the sedimentation velocity and equilibrium behavior of more complex interactions have now been developed. New applications of tracer sedimentation equilibrium experiments and the development of a fluorescence optical system for the analytical ultracentrifuge extend the accessible concentration range over several orders of magnitude and, coupled with the new analytical procedures, provide powerful new tools for studies of both weak and strong macromolecular interactions in solution.
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