The leader peptides from bacteriorhodopsin and halorhodopsin are potential membrane‐spanning amphipathic helices

We show that the N‐terminal leader peptides from the bacterial membrane proteins bacteriorhodopsin and halorhodopsin can be expected to form amphipathic α‐helices with a highly hydrophobic nonpolar face and a narrow, negatively charged polar face. This finding is discussed in terms of a model for the integration of these proteins into the bacterial membrane.