Unit

UNIT 4.8 The Use of Detergents to Purify Membrane Proteins

  1. Thomas Arnold,
  2. Dirk Linke

Published Online: 1 AUG 2008

DOI: 10.1002/0471140864.ps0408s53

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Arnold, T. and Linke, D. 2008. The Use of Detergents to Purify Membrane Proteins. Current Protocols in Protein Science. 53:4.8:4.8.1–4.8.30.

Author Information

  1. Max Planck Institute for Developmental Biology, Tübingen, Germany

Publication History

  1. Published Online: 1 AUG 2008
  2. Published Print: AUG 2008

This is not the most recent version of the article. View current version (1 APR 2016)

Abstract

Extraction of membrane proteins from biological membranes is usually accomplished with the help of detergents. This unit describes the use of detergents to solubilize and purify membrane proteins. The chemical and physical properties of the different classes of detergents typically used with biological samples are discussed. A separate section addresses the compatibility of detergents with applications downstream of the membrane protein purification process, such as optical spectroscopy, mass spectrometry, protein crystallography, or biomolecular NMR. Protocols in this unit include the isolation and solubilization of biological membranes, phase separation, and support protocols for detergent removal and detergent exchange using different methods. Curr. Protoc. Protein Sci. 53:4.8.1-4.8.30. © 2008 by John Wiley & Sons, Inc.

Keywords:

  • detergent;
  • membrane protein;
  • solubilization;
  • phase separation;
  • cloud point;
  • detergent removal;
  • detergent exchange