Gel chromatography and analytical ultracentrifugation to determine the extent of detergent binding and aggregation, and Stokes radius of membrane proteins using sarcoplasmic reticulum Ca2+–ATPase as an example-Reference-Cited by-同舟云学术

Gel chromatography and analytical ultracentrifugation to determine the extent of detergent binding and aggregation, and Stokes radius of membrane proteins using sarcoplasmic reticulum Ca2+–ATPase as an example

Published:2008-10-30 Issue:11 Volume:3 Page:1782-1795
ISSN:1754-2189
Container-title:Nature Protocols
language:en
Short-container-title:Nat Protoc

Author:

le Maire Marc,Arnou Bertrand,Olesen Claus,Georgin Dominique,Ebel Christine,Møller Jesper V

Publisher

Springer Science and Business Media LLC

Subject

General Biochemistry, Genetics and Molecular Biology

Link

http://www.nature.com/articles/nprot.2008.177.pdf

Reference48 articles.

1. Kragh-Hansen, U., le Maire, M. & Møller, J.V. The mechanism of detergent solubilization of liposomes and protein-containing membranes. Biophys. J. 75, 2932–2946 (1998).

2. le Maire, M., Champeil, P. & Møller, J.V. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta. 1508, 86–111 (2000).

3. Møller, J.V. & le Maire, M. Detergent binding as a measure of hydrophobic surface area of integral membrane proteins. J. Biol. Chem. 268, 18659–18672 (1993).

4. Lund, S. et al. Detergent structure and associated lipid as determinants in the stabilization of solubilized Ca2+-ATPase from sarcoplasmic reticulum. J. Biol. Chem. 264, 4907–4915 (1989).

5. Simons, K., Helenius, A. & Garoff, H. Solubilization of the membrane proteins from Semliki Forest virus with Triton X100. J. Mol. Biol. 80, 119–133 (1973).

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