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

Abstract

For structural studies of integral membrane proteins, including their 3D crystallization, the judicious use of detergent for solubilization and purification is required. Detergent binding by the solubilized protein is an important parameter to determine the hydrodynamic properties in terms of size and aggregational (monomeric/oligo(proto)meric) state of the… (More)
DOI: 10.1038/nprot.2008.177

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@article{Maire2008GelCA, title={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}, author={Marc le Maire and Bertrand Arnou and Claus Olesen and Dominique Georgin and Christine Maria Isabel Ebel and Jesper Vuust M\oller}, journal={Nature Protocols}, year={2008}, volume={3}, pages={1782-1795} }