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Helical preferences of alanine, glycine, and aminoisobutyric homopeptides
Author(s) -
Alemán Carlos,
Roca Ramón,
Luque F. Javier,
Orozco Modesto
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199705)28:1<83::aid-prot8>3.0.co;2-k
Subject(s) - aminoisobutyric acid , alanine , glycine , chemistry , amino acid , biophysics , biochemistry , biology
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. © 1997 Wiley‐Liss Inc.