for peptides. How peptides interact with the SDS micelle Binding affinities of tryptophan dipeptides, Trp-X (X Γ A, F, G, and how their structures change in the media have been I, K, L, S, T, V, W, and Y), X-Trp (X Γ A, F, G, K, L, P, R, V, discussed (5-7). Results indicating that some of the rela-W
The interaction of isomeric hexanediols with sodium dodecyl sulfate and dodecyltrimethylammonium bromide micelles
β Scribed by C. A. Kennedy; S. N. MacMillan; M. J. McAlduff; D. G. Marangoni
- Publisher
- Springer
- Year
- 2001
- Weight
- 123 KB
- Volume
- 279
- Category
- Article
- ISSN
- 0340-255X
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The interaction of slightly crosslinked gels of poly(diallyldimethylammonium bromide) (PDADMAB) with both the anionic surfactant sodium dodecyl sulfate (SDS) and the cationic surfactant cetylpyridinium bromide (CPB; system. name: __N__βhexadecylpyridinium bromide) in aqueous medium has
The recently reported data by Corti and Degiorgio for the diffusion coeffkients and micelle mo!ecular wei&ts of two surfactants were used for correiating the concentration dependence of hydrodynamic and thermodynamic properties of micelIar J+ticles. \_ Introduction ## Corti and Degiorgio [l] mea
## Abstract The free energies of transfer for indole and tryptophan derivatives and pentapeptides having single tryptophan residues from aqueous to sodium dodecyl sulfate (SDS) micellar phases have been systematically studied using the conventional method of ultraviolet absorption spectrophotometry