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Modeling of the α-helix conformation of homopeptides constituted by α-L-glutamic acid

✍ Scribed by David Zanuy; Carlos Alemán

Publisher
Wiley (John Wiley & Sons)
Year
1999
Tongue
English
Weight
159 KB
Volume
49
Category
Article
ISSN
0006-3525

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✦ Synopsis

The ␣-helix conformation of homopeptides constituted by ␣-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 ␣-L-glutamic acid has been compared with those of alanine and ␣-aminoisobutyric acid by analyzing cooperative energy effects. The influence of the solvent on the stability of the ␣-helix has been examined by using a self-consistent reaction field method. Finally, the stability of the ␣-helix conformation on the ionized homopeptides has been investigated.

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