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Title: Structural studies of bee melittin

Journal Article · · Biophys. J.; (United States)

The question of how proteins refold in passing from an aqueous phase to an amphipathic environment such as a membrane is beig addressed by a structural study of bee melittin. Melittin is the toxic, main protein of bee venom, and has been shown by others to integrate into natural and synthetic membranes and to lyse a variety of cells. This function is presumably related to its unusual sequence. Except for charges at the N-terminus and at lysine 7, the first 20 residues are largely apolar. In contrast, the last six residues contain four charges and two polar residues.

Research Organization:
Univ. of California, Los Angeles, CA (United States)
OSTI ID:
6761242
Journal Information:
Biophys. J.; (United States), Vol. 32:1
Country of Publication:
United States
Language:
English