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
Calorimetric Heat of the Helix-Coil Transition of Poly-L-glutamic Acid 1a
✍ Scribed by Rialdi, Giovanni; Hermans, Jan
- Book ID
- 126906913
- Publisher
- American Chemical Society
- Year
- 1966
- Tongue
- English
- Weight
- 220 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0002-7863
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📜 SIMILAR VOLUMES
Water-insoluble films (m. 0.04 X 3 X 30 mm.3 in dried state) of poly-Lglutamic acid (PGA), crosslinked with glycerol or polyvinyl alcohol at pH 4.8, were suspended in aqueous media and their relative lengths meaaured as a function of pH. The film elongate in alkaline pH and contract in acidic pH; th
## Abstract There have been many reports that the nuclear magnetic resonance (nmr) spectra of a large number of polypeptides exhibit peak doubling of the α‐carbon and the α‐carbon proton in the helix–coil transition region. One apparent exception to this generalization has been polypeptides with io
## 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