A Case Study of the Conformation of Poly(α-aminoisobutyric acid): α- or 3 10 -Helix
✍ Scribed by Prasad, B. V. Venkataram; Sasisekharan, V.
- Book ID
- 126909545
- Publisher
- American Chemical Society
- Year
- 1979
- Tongue
- English
- Weight
- 514 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0024-9297
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📜 SIMILAR VOLUMES
The anisotropic rotational motion of the backbone and the side chains of poly(t glutamic acid) in the a-helical structure was investigated using the ' G T , and T2 relaxation times of all carbon atoms with directly attached protons, obtained at a I T -Larmor frequency of 67.89 MHz. The evaluation of
The analysis of the factors that control the helical folding of Aib-rich peptides is extended to include sensitivity to sequence patterns, and in particular the presence of contiguous non-Aib a-mono-alkylated residues. The distinct hydrogen-bonding network of the 310helix, as contrasted with that of