Helical preferences of alanine, glycine, and aminoisobutyric homopeptides.
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.
Alemán
C
C
Departament d'Enginyeria Química, ETSEIB, Universitat Politècnica de Catalunya, Barcelona, Spain.
Roca
R
R
Luque
F J
FJ
Orozco
M
M
D000409:Alanine / Q000737:chemistry* / Q000378:metabolism; D000621:Aminoisobutyric Acids / Q000737:chemistry* / Q000378:metabolism; D002251:Carbon Tetrachloride; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005998:Glycine / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008962:Models, Theoretical; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011789:Quantum Theory; D012996:Solutions; D012997:Solvents / Q000737:chemistry; D013816:Thermodynamics
D000621:Aminoisobutyric Acids; D010446:Peptide Fragments; D012996:Solutions; D012997:Solvents; C100049:2-aminoisobutyric acid; D002251:Carbon Tetrachloride; D000409:Alanine; D005998:Glycine