Unit

UNIT 7.13 Methods for the Design and Analysis of Sedimentation Velocity and Sedimentation Equilibrium Experiments with Proteins

  1. Borries Demeler1,2

Published Online: 1 APR 2010

DOI: 10.1002/0471140864.ps0713s60

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Demeler, B. 2010. Methods for the Design and Analysis of Sedimentation Velocity and Sedimentation Equilibrium Experiments with Proteins. Current Protocols in Protein Science. 60:7.13:7.13.1–7.13.24.

Author Information

  1. 1

    Department of Biochemistry, The University of Texas Health Science Center at San Antonio, San Antonio, Texas

  2. 2

    Department of Computer Science, The University of Texas at San Antonio, San Antonio, Texas

Publication History

  1. Published Online: 1 APR 2010
  2. Published Print: APR 2010

Abstract

Analytical ultracentrifugation experiments play an integral role in the solution phase characterization of recombinant proteins and other biological macromolecules. This unit discusses the design of sedimentation velocity and sedimentation equilibrium experiments performed with a Beckman Optima XL-A or XL-I analytical ultracentrifuge. Optimal instrument settings and experimental design considerations are explained, and strategies for the analysis of experimental data with the UltraScan data analysis software package are presented. Special attention is paid to the strengths and weaknesses of the available detectors, and guidance is provided on how to extract maximum information from analytical ultracentrifugation experiments. Curr. Protoc. Protein Sci. 60:7.13.1-7.13.24. © 2010 by John Wiley & Sons, Inc.

Keywords:

  • analytical ultracentrifugation;
  • solution studies;
  • sedimentation velocity;
  • sedimentation equilibrium;
  • UltraScan;
  • 2-dimensional spectrum analysis;
  • absorbance optics;
  • intensity measurements