## 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
Nmr studies of poly-γ-benzyl-L-glutamate in trifluoroacetic/deuterochloroform solutions: Temperature dependence
✍ Scribed by E. Brosio; M. Delfini; A. De Paolis; M. Paci; F. Conti
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 245 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 carboxylic protons is reported.
📜 SIMILAR VOLUMES
## Abstract The helix–coil conformational transition undergone by poly(γ‐benzyl‐L‐glutamate) in solutions of trifluoroacetic acid and deuterated chloroform was studied by proton and carbon‐13 nmr. The results indicate that in the case of the solvent‐induced helix–coil transition, the side chain ass
## Abstract The coil to helix conformational transitions undergone by poly‐γ‐benzyl‐~L~‐glutamate in solutions of haloacetic acids and various cosolvents were studied by means of proton magnetic resonance. The results indicate a very small solvent dependence of the α‐CH Helix–coil chemical shift di
The helix-coil transition of poly(ybenzy1 L-glutamate) was studied by comparing proton magnetic relaxation behavior with optical activity studies. The transition temperatnre as determined by magnetic relaxation was lower than that obtained by optical activity. The relationship of these experiments