Expression of the isolated voltage sensing domain significantly alters its structural conformation as well as its gating kinetics, indicating the importance of studying the biological assembly in its entirety.
ArcLight, a popular optogenetic reporter of voltage, is studied at both single-molecule and macroscopic levels, which leads to new mechanistic understanding and to the rational design of a faster reporter.
The proteins Bax and Bak, which increase the permeability of the mitochondrial membrane during apoptosis, are also crucial for generating a mitochondrial membrane pore that is specifically involved in necrosis.
Single-molecule resolution of cAMP binding to the ligand binding domain of pacemaking channels in zero-mode waveguides reveals the dynamics of the distinct steps underlying both binding and isomerization of the binding domain.
The geometry selection rules of dynamic Min protein patterns are determined in fully confined fluidic chambers, showing that both oscillations and running waves are derivatives of spiral rotations that are established as the majority pattern.