Author(s): von Heijne G, Abrahmsn L, von Heijne G, Abrahmsn L
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Abstract Secretory signal peptides from individual prokaryotic and eukaryotic species have been analyzed, and the lengths and amino acid compositions of the positively charged amino-terminal region, the central hydrophobic region, and the carboxy-terminal cleavage-region have been compared. We find distinct differences between species in all three regions. Implications for protein secretion in foreign hosts are discussed.
This article was published in FEBS Lett
and referenced in Molecular Biology: Open Access