Domain structure of mitochondrial and chloroplast targeting peptides.

@article{Heijne1989DomainSO,
  title={Domain structure of mitochondrial and chloroplast targeting peptides.},
  author={Gunnar von Heijne and Johannes Steppuhn and Reinhold G. Herrmann},
  journal={European journal of biochemistry},
  year={1989},
  volume={180 3},
  pages={535-45}
}
Representative samples of mitochondrial and chloroplast targeting peptides have been analyzed in terms of amino acid composition, positional amino acid preferences and amphiphilic character. No highly conserved 'homology blocks' are found in either class of topogenic sequence. Mitochondrial-matrix-targeting peptides are composed of two domains with different amphiphilic properties. Arginine is frequently found either at position -10 or -2 relative to the cleavage site, suggesting that some… CONTINUE READING
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