Conformation of amino acid residue contiguous to helical polypeptide
Yoshiro Nakata, Toshihiro Akaike, Shohei Inoue
Abstract
Yoshiro Nakata, Toshihiro Akaike, Shohei Inoue
Abstract
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.
OpenAlex reports 2 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
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.
Key concepts: Chemistry, Residue (chemistry), Amino acid residue, Alanine, Polymer, Stereochemistry, Amino terminal, Amino acid