3
Figure 2: Detergent screen of HiTehA.
A) Representative thermal unfolding curves of HiTehA in 50 mM Tris HCl pH 8.0, 200 mM NaCl and the respective
detergents. B) Example for different unfolding onset temperatures in presence of C6E3 and DDM. C) Summary of Tm
values (red bars, right) and unfolding onset temperatures (black dots, right) in presence of different detergents.
The structure has gained great interest as TehA
shares limited sequence homology with the plant
anion channel proteins of the SLAC/SLAH family [7,
8]. The name-founding member of this plant anion
channel family, SLAC1 (slow anion channel 1),
alters the turgor pressure in guard cells in
accordance to release of the plant phytohormone
abscisic acid, thereby closing or opening the
stomata. The latter control the uptake of CO
2
required for efficient photosynthesis. However, as
open stomata also lead to water loss due to
transpiration, a stringent control of opening and
closing of these valves by altering the transport of
the anion channel is essential for the plant's
survival.
Results
Natively folded membrane proteins are most likely
obtained by extracting them out of plasma
membranes of the expression host by detergents.
The detergent used for proper solubilization might
interfere with stabilizing the protein in solution or is
inconvenient for crystallization or other subsequent
analysis processes thus requiring a detergent
exchange during purification. As determining the
best-suited detergent is an empirical process for
