Methods to predict which portions of Alpha helices are exposed to water, to protein, or to lipid were developed and refined. These methods were tested on proteins of known structure, specifically the globin family, and found to successfully classify most residues as buried, partially buried, or exposed. The methods also yield results consistent with experimental findings regarding which residues in bacteriorhodopsin are exposed to water, buried inside the protein, or exposes to lipid. The method was used with other factors to construct new molecular models for colicin A and colicin E1 membrane channels. This construction process is difficult and is only possible if there are sufficient experimental facts known about the structure. With these methods, it is now possible to screen proteins for probable channel forming properties.