Chain conformation in polyretropeptides III: Design of a 310 helix using α,α-dialkylated amino acids and retropeptide bonds
✍ Scribed by Carlos Alemán
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 139 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
Computer simulations have been used to design a polypeptide with a 3 10 helix conformation. The study has been been performed taking advantage of the intrinsic helix forming tendency of ␣-Aminoisobutyric acid. In order to avoid the formation of the ␣ helix, which is the other common helical conformation adopted by ␣-Aminoisobutyric acidbased peptides, retropeptide bonds have been included in the sequence. Thus, retropeptides are not able to form the intramolecular hydrogen bonding interactions characteristic of the ␣ helix. The influences of both the peptide length and the solvent have been examined and compared with those of the polypeptide without retropeptide bonds. Proteins