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Modeling of the α‐helix conformation of homopeptides constituted by α‐ L ‐glutamic acid
Author(s) -
Zanuy David,
Alemán Carlos
Publication year - 1999
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/(sici)1097-0282(199905)49:6<497::aid-bip7>3.0.co;2-9
Subject(s) - chemistry , helix (gastropod) , glutamic acid , alanine , stereochemistry , amino acid , crystallography , biochemistry , ecology , snail , biology
The α‐helix conformation of homopeptides constituted by α‐ L ‐glutamic acid has been modeled by means of quantum mechanical methods. The results have allowed us to obtain a detailed description not only of the helical backbone, but also of the conformational preferences of the side chains. The intrinsic helix forming tendency of α‐ L ‐glutamic acid has been compared with those of alanine and α‐aminoisobutyric acid by analyzing cooperative energy effects. The influence of the solvent on the stability of the α‐helix has been examined by using a self‐ consistent reaction field method. Finally, the stability of the α‐helix conformation on the ionized homopeptides has been investigated. © 1999 John Wiley & Sons, Inc. Biopoly 49: 497–504, 1999