Hydrogen bonding in peptide secondary structures

Z. Varga, Attila Kovács

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)302-312
Number of pages11
JournalInternational Journal of Quantum Chemistry
Volume105
Issue number4
DOIs
Publication statusPublished - Nov 15 2005

Fingerprint

peptides
Hydrogen bonds
Peptides
helices
hydrogen
Valine
Serine
interactions
hydrogen bonds
Oligopeptides
alanine
glycine
Amides
Alanine
Glycine
amides
ribbons
Structural properties
Substitution reactions
substitutes

Keywords

  • Conformation
  • COSMO solvation calculations
  • Density functional theory
  • Homo-oligopeptides
  • Hydrogen bonding

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Hydrogen bonding in peptide secondary structures. / Varga, Z.; Kovács, Attila.

In: International Journal of Quantum Chemistry, Vol. 105, No. 4, 15.11.2005, p. 302-312.

Research output: Contribution to journalArticle

Varga, Z. ; Kovács, Attila. / Hydrogen bonding in peptide secondary structures. In: International Journal of Quantum Chemistry. 2005 ; Vol. 105, No. 4. pp. 302-312.
@article{3a7a9c7c60dd49c0bc4bf790fff6a4c0,
title = "Hydrogen bonding in peptide secondary structures",
abstract = "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.",
keywords = "Conformation, COSMO solvation calculations, Density functional theory, Homo-oligopeptides, Hydrogen bonding",
author = "Z. Varga and Attila Kov{\'a}cs",
year = "2005",
month = "11",
day = "15",
doi = "10.1002/qua.20706",
language = "English",
volume = "105",
pages = "302--312",
journal = "International Journal of Quantum Chemistry",
issn = "0020-7608",
publisher = "John Wiley and Sons Inc.",
number = "4",

}

TY - JOUR

T1 - Hydrogen bonding in peptide secondary structures

AU - Varga, Z.

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 - Conformation

KW - COSMO solvation calculations

KW - Density functional theory

KW - Homo-oligopeptides

KW - Hydrogen bonding

UR - http://www.scopus.com/inward/record.url?scp=30544450252&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=30544450252&partnerID=8YFLogxK

U2 - 10.1002/qua.20706

DO - 10.1002/qua.20706

M3 - Article

AN - SCOPUS:30544450252

VL - 105

SP - 302

EP - 312

JO - International Journal of Quantum Chemistry

JF - International Journal of Quantum Chemistry

SN - 0020-7608

IS - 4

ER -