## 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
13C and 1H NMR studies of helix-coil transition of poly(β-benzyl-L-aspartate) and poly(γ-benzyl-L-glutamate): Behavior in nonprotonating solvent mixtures, and origin of solvent-induced chemical shift
✍ Scribed by Yasuyuki Suzuki; Yoshio Inoue; Riichirô Chûjô
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1977
- Tongue
- English
- Weight
- 574 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
From the results of ^13^C‐nmr measurement of poly(β‐benzyl‐L‐aspartate) and its model compounds in dimethyl sulphoxide/deuterated chloroform mixtures, it was found that the side chain of poly(β‐benzyl‐L‐aspartate) is solvated by dimethyl sulphoxide in the region more than dimethyl sulphoxide 20% (v/v), where the backbone maintains the α‐helix. The chemical shift differences in the benzyl group carbons of poly(γ‐benzyl‐L‐glutamate) (trifluoroacetic acid/deuterated chloroform) accompanied by the helix‐coil transition, originate from the interaction between the ester group of the side chain and trifluoroacetic acid. The chemical shift difference in the ester carbon is similar. On the other hand, the chemical shift differences of the side‐chain carbons in the alkyl portion (C^β^, C^γ^) originate not only from the interaction between the ester group of the side chain and trifluoroacetic acid, but also from some other unknown factors. The chemical shift differences of the side‐chain carbons of poly(β‐benzyl‐L‐aspartate) originate from the interaction between the ester group of the side chain and trifluoroacetic acid.
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The helix-coil transition for poly(P-benzyl-L-aspartate) [poly(Asp[OBzl])] in solvent mixtures of trifluoroacetic acid/deuterated chloroform (F3AcOH/CDC13) was studied by means of proton and carbon-13 nmr. Conformational fixation of the side chain occurs before the coil-helix transition of the backb
## Abstract The dielectric absorption of poly‐DL‐phenylalanine and poly‐γ‐benzyl‐L‐aspartate (PLAB) was measured in very dilute solutions to determine the type of molecular association and to locate the helix–coil transition. Both polypeptides were present as associated helices in chloroform. The m