Stabilizing membrane proteins.
Membrane proteins can be extremely stable in a bilayer environment, but are often unstable and rapidly lose activity after detergent solubilization. Poor stability can preclude the detailed characterization of many membrane proteins. One way to alleviate this problem is to find more stable mutants of a membrane protein of interest. This approach is made tractable by the finding that stability-enhancing mutations appear to be relatively common in membrane proteins.
Bowie
J U
JU
Department of Chemistry and Biochemistry, and UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Boyer Hall, 611 Charles E Young Drive East, Los Angeles, CA 90095-1570, USA. bowie@mbi.ucla.edu
D003902:Detergents; D004795:Enzyme Stability / Q000235:genetics*; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D012995:Solubility
D003902:Detergents; D008051:Lipid Bilayers; D008565:Membrane Proteins