Effect of micellar charge on the conformation and dynamics of melittin
β Scribed by H. Raghuraman; Amitabha Chattopadhyay
- Book ID
- 105946069
- Publisher
- Springer
- Year
- 2004
- Tongue
- English
- Weight
- 341 KB
- Volume
- 33
- Category
- Article
- ISSN
- 1432-1017
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π SIMILAR VOLUMES
A 15-residue hybrid peptide ( KWKLFKKIGAVLKVL-amide) incorporating partial sequences of cecropin A and melittin causes the release of carboxyfluoresceine encapsulated in phosphatidylcholine liposomes. Succinylation of the amino groups in the N-terminus and lysine side chains inhibits the effect of t
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