Analysis of detergent-solubilized membrane proteins in the analytical ultracentrifuge

Neal C Robinson, Baltazar Gomez, Andrej Musatov, Jaime Ortega-Lopez

Resultado de la investigación: Review articlerevisión exhaustiva

12 Citas (Scopus)

Resumen

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.

Idioma originalEnglish (US)
Páginas (desde-hasta)960-968
Número de páginas9
PublicaciónChemtracts
Volumen11
N.º13
EstadoPublished - 1998

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry
  • Molecular Biology

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