ISSN:
1476-4687
Source:
Nature Archives 1869 - 2009
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
Notes:
[Auszug] Figure 1 shows the structure of melittin7. It is a cationic, amphipathic peptide in which residues 1-20 are predominantly hydrophobic and residues 21-26 hydrophilic. Melittin is surface-active and has been shown to disrupt cell membranes and artificial phospholipid liposomes8'9. Unmodified melittin ...
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1038/267713a0