Proposed knobs-into-holes packing for several membrane proteins.
We investigated the possible side chain/side chain interactions of four potential transmembrane proteins. The basic assumptions are that the proteins are alpha-helical, and that the proteins aggregate with knobs-into-holes packing. It was found that these four proteins can be assembled into stereochemically feasible bundles of alpha-helices with hydrophobic exteriors and with hydrogen bonds between the side chains of one alpha-helix and the side chains of its knobs-into-holes packed neighbors.
D001435:Bacteriophages / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry; D002213:Capsid / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry; D006021:Glycophorins / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008074:Lipoproteins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D010457:Peptidoglycan / Q000737:chemistry; D017433:Protein Structure, Secondary
D006021:Glycophorins; D008074:Lipoproteins; D008565:Membrane Proteins; D010457:Peptidoglycan; D001436:Bacteriorhodopsins