Disposition of polar and nonpolar residues on outer surfaces of transmembrane helical segments of proteins involved in proton translocation.
"Helical wheel" projections of transmembrane helical segments of membrane proteins involved in proton translocation were constructed. The particular proteins studied were the uncF protein subunit of the Escherichia coli proton-ATPase, the uncE protein subunit of the E. coli proton-ATPase, and cytochrome oxidase subunit III. Clear demarcation of polar and nonpolar regions on surfaces of transmembrane helical segments was seen in the uncF protein and in uncE protein helical segment two, but not in uncE protein helical segment one. The transmembrane segment of cytochrome oxidase subunit III which includes the dicyclohexylcarbodiimide (DCCD)-reactive residue was very similar to E. coli uncE protein helical segment two. The DCCD-reactive residue in both was clearly located on a nonpolar surface.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D003576:Electron Transport Complex IV / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000378:metabolism; D011522:Protons; D013499:Surface Properties
D001426:Bacterial Proteins; D008565:Membrane Proteins; D011522:Protons; D003576:Electron Transport Complex IV; D006180:Proton-Translocating ATPases