Abstract
The transduction of electric fields into protein motion plays an essential role in the generation and propagation of cellular signals. Voltage‐sensing domains (VSD) carry out these functions through reorientations of discrete gating charges in the S4 helix. The voltage sensitive phosphatase from C. intestinalis (Ci‐VSP) is controlled by a standard VSD with high sequence similarity to the S1‐S4 segments found in Na+ and K+ channels. To address some of the fundamental questions regarding how membrane proteins sense transmembrane voltages, we have pursued structural and biophysical information on Ci‐VSP’s isolated VSD, under conditions that stabilize the Up and the Down conformations. These will be discussed in the context of explicit mechanisms for voltage sensing.
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