title: Mitochondrial targeting sequences. Why 'non-amphiphilic' peptides may still be amphiphilic.
abstract: The notion that mitochondrial targeting peptides form amphiphilic alpha-helices with one apolar and one polar, positively charged face is controversial, since some experimental results seem to imply that non-amphiphilic targeting peptides can also function as import signals. However, the standard methods used to assess the amphiphilicity of a peptide may be misleading, since they do not take the flexibility of the amino acid side chains into account. To demonstrate this, we have developed a new method for calculating the amphiphilicity of helical peptides.
authors.affiliation: Department of Theoretical Physics, Royal Institute of Technology, Stockholm, Sweden.
authors.forename: Y
authors.initials: Y
authors.lastname: Gavel
authors.forename: L
authors.initials: L
authors.lastname: Nilsson
authors.forename: G
authors.initials: G
authors.lastname: von Heijne
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008928:Mitochondria / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation
chemical_list: D000596:Amino Acids; D010455:Peptides