Theoretical Study on Side-Chain Control of the 14-Helix and the 10/12-Helix of β-Peptides
✍ Scribed by Wu, Yun-Dong; Wang, De-Ping
- Book ID
- 127100388
- Publisher
- American Chemical Society
- Year
- 1999
- Tongue
- English
- Weight
- 376 KB
- Volume
- 121
- Category
- Article
- ISSN
- 0002-7863
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## Abstract A systematic analysis of the substituent influence on the formation of the unique secondary structure type of “mixed” helices in the homologous α‐, β‐, and γ‐peptides was performed on the basis of ab initio molecular orbital theory. Contrary to the common periodic peptide helices, mixed
A peptide fragment corresponding to the third helix of Staphylococcus Aureus protein A, domain B, was chosen to study the effect of the main-chain direction upon secondary structure formation and stability, applying the retro-enantio concept. For this purpose, two peptides consisting of the native (