Study of polytopic membrane protein topological organization as a function of membrane lipid composition.
| Data(s) |
01/01/2010
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|---|---|
| Resumo |
A protocol is described using lipid mutants and thiol-specific chemical reagents to study lipid-dependent and host-specific membrane protein topogenesis by the substituted-cysteine accessibility method as applied to transmembrane domains (SCAM). SCAM is adapted to follow changes in membrane protein topology as a function of changes in membrane lipid composition. The strategy described can be adapted to any membrane system. |
| Identificador |
http://digitalcommons.library.tmc.edu/uthmed_docs/204 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3099133/?tool=pmcentrez |
| Publicador |
DigitalCommons@The Texas Medical Center |
| Fonte |
UT Medical School Journal Articles |
| Palavras-Chave | #Bacterial Proteins #Blotting #Western #Electrophoresis #Polyacrylamide Gel #Glycosyltransferases #Immunoprecipitation #Membrane Lipids #Membrane Proteins #Membrane Transport Proteins #Phosphatidylethanolamines #Phospholipids #Blotting, Western #Electrophoresis, Polyacrylamide Gel #Medicine and Health Sciences |
| Tipo |
text |
