Positional preference of proline in α-helices
✍ Scribed by Kim, Mee Kyoung (author);Kang, Young Kee (author)
- Book ID
- 111753657
- Publisher
- Wiley
- Year
- 1999
- Tongue
- English
- Weight
- 406 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0961-8368
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The disrupting effect of a prolyl residue on an a-helix has been analyzed by means of conformational energy computations. In the preferred, nearly a-helical conformations of Ac-Ala,-Pro-NHMe and of Ac-Ala7-Pro-Ah7-NHMe, only the residue preceding Pro is not a-helical, while all other residues can oc
An analysis of the amino acid distributions at 15 positions, viz., NЉ, NЈ, Ncap, N1, N2, N3, N4, Mid, C4, C3, C2, C1, Ccap, CЈ, and CЉ in 1,131 ␣-helices reveals that each position has its own unique characteristics. In general, natural helix sequences optimize by identifying the residues to be avoi