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Mitochondrial targeting sequences why ‘non‐amphiphilic’ peptides may still be amphiphilic
Author(s) -
Gavel Ylva,
Nilsson Lennart,
von Heijne Gunnar
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81257-2
Subject(s) - amphiphile , peptide , chemistry , function (biology) , amino acid , biophysics , biochemistry , flexibility (engineering) , combinatorial chemistry , biology , organic chemistry , microbiology and biotechnology , copolymer , polymer , statistics , mathematics
The notion that mitochondrial targeting peptides form amphiphilic α‐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.