Hydrodynamic analysis of detergent-solubilized membrane proteins and protein complexes in the analytical ultracentrifuge is similar in principle to that of normal soluble proteins. However, caution must be exercised in choosing an appropriate solubilizing detergent and in interpreting the data. Accurate protein molecular weights can be obtained and self-association can be studied, but proper corrections for bound detergent are essential. However, it is usually not possible to obtain useful information of protein size or shape since the frictional coefficient is often dominated by the hydrodynamic size of the bound detergent.
|Original language||English (US)|
|Number of pages||9|
|State||Published - Jan 1 1998|
ASJC Scopus subject areas
- Molecular Biology