## Abstract The calculation of the conformational energy of the terminal D‐ or L‐alanine residue contiguous to an α‐helical polypeptide, polyalanine, was made. Both L‐and D‐residues contiguous to the carboxyl terminal of α‐helical poly(L‐alanine) are considered to prefer the α‐helical conformation
An obligatory α-helical amino acid residue
✍ Scribed by Antony W. Burgess; Sydney J. Leach
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 393 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Stereochemical studies predict that α‐amino isobutyric acid, one of the amino acids found in antibiotics, can fold only into left‐ or righthanded α‐helical conformations. Such residues will direct chain folding and should be useful in synthetic analogs of protein sequences to increase helix stability.
📜 SIMILAR VOLUMES
## Abstract Relevant parameters and stereochemical consequences of helices [α‐helix, 3~10~‐helix, β‐bend ribbon spiral, γ‐helix, 2.0~5~‐helix, poly(Pro)~__n__~ type‐I and ‐II helices, and collagen triple helix] of peptides based on α‐amino acids for use as templates in various branches of chemistry
## Abstract Linear and cyclic cyclolinopeptide A (CLA) analogues containing α‐hydroxymethylleucine (HmL) in positions 1, 4, and 1&4, and α‐hydroxymethylvaline (HmV) in position 5, were synthesized by the solid‐phase peptide strategy and cyclized with the 1‐Ethyl‐3‐(3‐dimethylaminopropyl)‐carbodiimi
Scheme 1. Treatment of the (E)-azobenzene peptide 1 a and of its Z isomer 1 b at 25 8C in 100 mm phosphate buffer (pH 7.0) with GSH/GSSG.