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The Structures of Some Peptides from Bee Venom

✍ Scribed by Jack GAULDIE; Jennifer M. HANSON; Rudolf A. SHIPOLINI; Charles A. VERNON


Book ID
115116490
Publisher
John Wiley and Sons
Year
1978
Tongue
English
Weight
490 KB
Volume
83
Category
Article
ISSN
1432-1327

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## Abstract The circular dichroism (CD) and ^1^H‐nmr properties of peptide 401, a bee venom component with 22 amino acid residues and two disulfide bridges, have been studied under a variety of conditions and compared with those of the structurally related octadecapeptide apamin. The major componen

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In aqueous solution, melittin structure, investigated by CD and 'H-nmr, depends on pH and ionic composition, which also regulate the aggregation state of the peptide. When interacting with phospholipids, however, melittin exhibits a right-handed helical conformation without any evidence of oligomeri