The objective has been to establish if those ions which are known to change the stability of the struct,ure of proteins, have any influence on the properties of ionizable polypeptides. Potentiometric titrations and complementary optical rotation data are presented for aqueous solutions of poly-L-lys
Dilatometric and refractometric studies of the helix—coil transition of poly-L-glutamic acid in aqueous solution
✍ Scribed by Hajime Noguchi; Jen Tsi Yang
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1963
- Tongue
- English
- Weight
- 663 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0006-3525
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📜 SIMILAR VOLUMES
The folding of randomly coiled poly(bg1utamic acid) to the helical state has been studied in N-methylacetamide by titration methods. Since this solvent would be expected to form amide-peptide group hydrogen bonds with the unfolded form of the polymer, to a first approximation no helix stabilization
## Abstract The rate of conformational change of aqueous poly(α‐L‐lysine) solutions was measured using the electric field pulse relaxation method with conductivity detection. The relaxation time as a function of pH exhibits two maxima. One is assigned to a proton transfer reaction and the other to
Chimica delle Macromolecole (CNR) Sex. ZZZ, Ztaly ## Synopsis Further direct evidences are given that a clear correlation exists between potentiometric and spectroscopic measurements in monitoring the poly( bglutamic acid) helix + coil transition. Specific Li + ion poly(r,-glutamic acid) interact