The Structures of Some Peptides from Bee Venom
β 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
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The circular dichroism (CD) and ^1^Hβnmr 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
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