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 alpha-helics 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.
D001436:Bacteriorhodopsins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D006217:Halobacterium / Q000378:metabolism; D025602:Halorhodopsins; D008954:Models, Biological; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000378:metabolism*
D025602:Halorhodopsins; D021382:Protein Sorting Signals; D001436:Bacteriorhodopsins