The conformation of melittin, a surface-active polypeptide, in solution was studied by CD spectra between 190 and 240 nm. The molecule was essentially unordered (possibly with a trace of helix) in water without salt at neutral pH. Upon deprotonation of four of the six cationic groups a t pH 12 the p
β¦ LIBER β¦
Conformation and aggregation of melittin: dependence of pH and concentration
β Scribed by Bello, Jake; Bello, Helene R.; Granados, Edward
- Book ID
- 120615446
- Publisher
- American Chemical Society
- Year
- 1982
- Tongue
- English
- Weight
- 676 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0006-2960
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