## Abstract The ir spectra of σ–nitrophenylthio‐tetra‐ and hexa‐γ‐benzyl‐L‐glutamate ethylamides were measured at different concentrations in chloroform and ethylene dichloride. The molar extinction coefficients of two bands, each for the amide I and A modes, were observed as indicating the content
Structure of micelles formed by monodisperse hexa-(γ-benzyl-L-glutamate) in solution
✍ Scribed by Toyoko Imae; Kenji Okahashi; Shoichi Ikeda
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 653 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The angular dependence of light scattering and the concentration dependence of the relative viscosity have been measured in solutions of o‐nitrophenylthio‐hexa‐(γ‐benzyl‐L‐glutamate) ethylamide in ethylene dichloride. Both the reduced intensity of scattered light and the reduced viscosity of the solution suddenly increase above a certain critical concentration, below which both of them remain low and constant. The Debye plot of light scattering indicates that primary micelles having an aggregation number 48 are formed at the critical micelle concentration and that secondary micelles, each consisting of 294 molecules, then appear in increasing amounts with increasing concentration beyond the critical micelle concentration. The secondary micelle is rodlike and has a length of 1170 Å, if it is rigid. An analysis of the reduced viscosity leads to the intrinsic viscosity for the primary micelle, 0.360 dL g^−1^, and to that of the secondary micelle, 1.28 dL g^−1^. If the secondary micelle is represented by a prolate ellipsoid, it should have an axial ratio of 47. If the polypeptide chains are extended in the micelle, the observed aggregation number and axial ratio of the secondary micelle can well accommodate the intermolecularly hydrogen‐bonded in‐register β‐structure of anti‐parallel chains. In the primary micelle, some folded polypeptide chains are involved, and an intermolecularly hydrogen‐bonded out‐of‐register structure would form a rather open network.
📜 SIMILAR VOLUMES
## Abstract The present communication describes a new way of studying helix–random coil transformations of polypeptide, poly‐(γ‐benzyl L‐glutamate), in benzene–trifluoracetic acid (TFA) and chloroform–TFA systems. The difference between the PMR chemical shift of TFA with and without the polypeptide
Light scattering from ethylene dichloride solutions of tetra-(y-benzyl-cglutamate)s has been measured and their association in solution is examined. One of the peptides is monodisperse o-nitrophenylthio-tetra-(y-benzyl-cglutamate) ethylamide prepared by a stepwise condensation method, and the other
The electrorheological (ER) effect of an anisotropic solution of poly( g-benzyl-L-glutamate) (PBLG) in 1,4-dioxane with a concentration of 15 wt % was measured at a shear rate of 2.6 s 01 by our parallel-plate sliding rheometer. The solution under shear flow was stimulated by stepwise electric field
## Abstract The helix–random‐coil transition process for poly‐γ‐benzyl‐L‐glutamate (PBG) in solvent mixtures trifluoroacetic acid/deuterochloroform (TFA/CDCl~3~) at different temperatures has been studied by nmr. The chemical shift behavior of the α‐CH resonances of the peptide chain and of the TFA
Nine samples of poly-ybeneyl-kglutamate (PBLG), ranging in aw from 19,000 to 410,000, were examined viscometrically and by ultracentrifugation with dimethylformamide (DMF) at 25°C. as helicogenic solvent. The data for [v] and SO (limiting sedimentation coefficient) as functions of am were fitted wel