In this paper two points are considered: the methods of evaluating the helical content 8 and the calculation of the parameters of the transition from experimental data and its interpretation. The parameter AH obtained is in good agreement with the calorimetric one and v is found to be independent of
Radiation effects of poly(l-glutamic acid) and poly(l-lysine) in the helix-coil transitional state
✍ Scribed by Mitsuo Ishikawa; K. Takakura
- Publisher
- Springer-Verlag
- Year
- 1976
- Tongue
- English
- Weight
- 415 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0301-634X
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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
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 A polarimetric electric‐field‐jump relaxation apparatus is described and used to determine the relaxation spectrum for the helix–coil transition of poly(α,L‐glutamic acid) in water at 24°C. A maximum relaxation time of 1.7 μc occurs at the transition midpoint (pH = 5.9) yielding a rate
## Abstract The thermal helix–coil transition of poly(γ‐benzyl L‐glutamate‐__co__‐ε‐carbobenzoxy‐L‐lysine) copolypeptides was studied in solvent mixtures of different compositions. The cooperativity parameter __v__ changes linearly with polymer (and solvent) composition, whereas the heat of the tra