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Conformation of amino acid residue contiguous to helical polypeptide
Author(s) -
Nakata Yoshiro,
Akaike Toshihiro,
Inoue Shohei
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170411
Subject(s) - chemistry , residue (chemistry) , amino acid residue , alanine , polymer , stereochemistry , amino terminal , amino acid , crystallography , terminal (telecommunication) , peptide sequence , biochemistry , organic chemistry , gene , telecommunications , computer science
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.