title: Statistical and functional analyses of viral and cellular proteins with N-terminal amphipathic alpha-helices with large hydrophobic moments: importance to macromolecular recognition and organelle targeting.
abstract: A total of 1,911 proteins with N-terminal methionyl residues were computer screened for potential N-terminal alpha-helices with strong amphipathic character. By the criteria of D. Eisenberg (Annu. Rev. Biochem. 53:595-623, 1984), only 3.5% of nonplastid, nonviral proteins exhibited potential N-terminal alpha-helices, 18 residues in length, with hydrophobic moment values per amino acyl residue ([muH]) in excess of 0.4. By contrast, 10% of viral proteins exhibited corresponding [muH] values in excess of 0.4. Of these viral proteins with known functions, 55% were found to interact functionally with nucleic acids, 30% were membrane-interacting proteins or their precursors, and 15% were structural proteins, primarily concerned with host cell interactions. These observations suggest that N-terminal amphipathic alpha-helices of viral proteins may (i) function in nucleic acid binding, (ii) facilitate membrane insertion, and (iii) promote host cell interactions. Analyses of potential amphipathic N-terminal alpha-helices of cellular proteins are also reported, and their significance to organellar or envelope targeting is discussed.
authors: Department of Biology, University of California, San Diego, La Jolla 92093.
authors: M H
authors: MH
authors: Saier
authors: P
authors: P
authors: McCaldon
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis / Q000502:physiology*; D008715:Methionine / Q000378:metabolism; D009940:Organoids / Q000032:analysis; D011487:Protein Conformation; D012984:Software; D014764:Viral Proteins / Q000032:analysis / Q000502:physiology*
chemical_list: D008565:Membrane Proteins; D014764:Viral Proteins; D008715:Methionine