Limits of Proteomics: Protein Solubilisation Issues
Published Online: 15 MAR 2012
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Rabilloud, T. 2012. Limits of Proteomics: Protein Solubilisation Issues. eLS. .
- Published Online: 15 MAR 2012
Because of their tremendous chemical heterogeneity, many proteins, such as membrane proteins, are poorly soluble in aqueous solvents. This precludes their analysis by classical proteomics techniques, whether these techniques are based on protein separation (e.g. two-dimensional gel-based proteomics) or on peptide separation after in-solution digestion. For techniques based on peptide separation, the issue is to couple on the one side a complete solubilisation of proteins, a good efficiency of the protease used to produce the peptides, and on the other side minimal interference with the techniques used to separate the peptides. For techniques based on protein separation, the issue is to solubilise the proteins and to keep them soluble under the conditions used for the protein separation. For both type of technologies, combinations of detergents and chaotropes often provide the most performing solution to the protein solubilisation problem, although complete solubilisation can never be guaranteed.
Proteins must be extracted from their cellular context into an aqueous-based solvent for their analysis.
Surfactants/detergents provide the adequate medium to mimic a lipid-like environment in water.
The structural variety of detergents provides the various solubilisation performances that can be adapted to many proteomics methods.
Chaotropes are often used in conjunction with detergents to improve protein/peptide solubility.