Membrane proteins can be extremely stable in a bilayer environment, but are
often unstable and rapidly lose activity after detergent solubilization. P
oor stability can preclude the detailed characterization of many membrane p
roteins. One way to alleviate this problem is to find more stable mutants o
f a membrane protein of interest. This approach is made tractable by the fi
nding that stability-enhancing mutations appear to be relatively common in
membrane proteins.