Helical preferences of alanine, glycine, and aminoisobutyric homopeptides

TitleHelical preferences of alanine, glycine, and aminoisobutyric homopeptides
Publication TypeJournal Article
Year of Publication1997
AuthorsAleman, C, Roca R, Luque FJ, Orozco M
Pagination83 - 93
Date Published1997/05//
KeywordsAlanine/chemistry/metabolism; Aminoisobutyric Acids/chemistry/metabolism; Carbon Tetrachloride; Chemistry, Molecular; Models, Physical; Glycine/chemistry/metabolism; Models, Secondary; Quantum Theory; Solutions; Solvents/chemistry; Thermodynamics, Theoretical; Peptide Fragments/chemistry; Physicochemical Phenomena; Protein Structure

The stability between helical conformations of homopeptides of alanine, glycine, and aminoisobutyric acid has been studied by means of quantum-mechanical methods. The influence of peptide length on the relative stability between helical conformations has also been analyzed by means of systematic studies for peptides of size up to 11 residues. Finally, the influence of the solvent has been examined by using self-consistent reaction field methods. The results provide a detailed picture of the modulation exerted by these factors on the helical preferences of these peptides.