TY - JOUR
T1 - Hydrogen bonding in peptide secondary structures
AU - Varga, Zoltán
AU - Kovács, Attila
PY - 2005/11/15
Y1 - 2005/11/15
N2 - Hydrogen bonding interactions in various peptide secondary structures (β-sheet, 27-ribbon, 310-helix, α-helix, π-helix, β-turn II, and γ-turn) have been investigated in small oligopeptides by quantum chemical calculations at the B3LYP/6-31G** level. Besides the primary O⋯H-N interactions, the optimized structures revealed the importance of N⋯H-N hydrogen bonding in several structures. The effect of substitution on the energy and structural properties was investigated comparing the properties of glycine, alanine, valine, and serine. The aliphatic substituents generally weaken the hydrogen bonds, the strongest effects being observed in crowded valine conformers. Additional hydrogen bonding interactions introduced by the OH group of serine can both strengthen (by polarizing the amide moiety through N⋯H interaction) and weaken (constraining the C=O oxygen by O⋯H-O interaction) the backbone hydrogen bonds. The effect of water as a polarizable medium on the energy properties was assessed by the COSMO model.
AB - Hydrogen bonding interactions in various peptide secondary structures (β-sheet, 27-ribbon, 310-helix, α-helix, π-helix, β-turn II, and γ-turn) have been investigated in small oligopeptides by quantum chemical calculations at the B3LYP/6-31G** level. Besides the primary O⋯H-N interactions, the optimized structures revealed the importance of N⋯H-N hydrogen bonding in several structures. The effect of substitution on the energy and structural properties was investigated comparing the properties of glycine, alanine, valine, and serine. The aliphatic substituents generally weaken the hydrogen bonds, the strongest effects being observed in crowded valine conformers. Additional hydrogen bonding interactions introduced by the OH group of serine can both strengthen (by polarizing the amide moiety through N⋯H interaction) and weaken (constraining the C=O oxygen by O⋯H-O interaction) the backbone hydrogen bonds. The effect of water as a polarizable medium on the energy properties was assessed by the COSMO model.
KW - COSMO solvation calculations
KW - Conformation
KW - Density functional theory
KW - Homo-oligopeptides
KW - Hydrogen bonding
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U2 - 10.1002/qua.20706
DO - 10.1002/qua.20706
M3 - Article
AN - SCOPUS:30544450252
SN - 0020-7608
VL - 105
SP - 302
EP - 312
JO - International Journal of Quantum Chemistry
JF - International Journal of Quantum Chemistry
IS - 4
ER -