## Abstract Acetyl‐(dehydro‐Phe) and acetyl‐bis(dehydro‐Phe) groups have been attached to the ε‐amino group of the lysine residues of the copolymer poly(Glu^92^Lys^8^) by reacting this last with acetyl‐(dehydro‐Phe)‐azlactone and acetyl‐bis(dehydro‐Phe)‐azlactone, respectively. In the latter case
Conformation of amino acid residue contiguous to helical polypeptide
✍ Scribed by Yoshiro Nakata; Toshihiro Akaike; Shohei Inoue
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 288 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 due to the effect of the α‐helical structure of the polymer. The residue at the amino terminal is found to be less affected by the α‐helical structure of the polymer.
📜 SIMILAR VOLUMES
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