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BAR domains bend membranes by imposing their curved shape. In this issue, Isas et al. show the structural differences in the interaction of the BAR domain protein amphiphysin with vesicles and tubes. They find that superficial interactions lead to vesicles, whereas more penetrating interactions of a more crowded protein lead to tubes.
Site-directed spin labeling of proteins is experiencing a phase of rapid technical evolution, application and evaluation. New strategies have been introduced for determining membrane protein topography, electrostatic potentials, the orientation of proteins at membrane surfaces and inter-residue distances. New applications include studies of β strands, structure mapping using spin-spin interactions,...
In voltage-dependent K+ channels, each of the four identical subunits contributes one pore loop to the central ion selectivity unit at the interface between the subunits. The pore loop is also the target for scorpion venom peptide inhibitors. These inhibitors bind at the pore entryway between the four subunits and can assume any one of four orientations. The orientations become distinguishable only...
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