[Double and bifurcated hydrogen bonds in alpha-helices of globular proteins]

Biofizika. 2001 Nov-Dec;46(6):969-77.
[Article in Russian]

Abstract

The statistical analysis of hydrogen bonds distribution in space structures of globular proteins has been done. The parameters of H-bonds in the different secondary structures of globular proteins were collected. In alpha-helices besides the canonical 1-5 H-bonds (the mean length 3 A), 1-4 H-bonds were observed (the mean length 3.2 A). The histograms of length and angular distributions of the bonds are presented. It was found on the basis of quantum chemistry calculations that most H-bonds in alpha-helices are double or bifurcated.

Publication types

  • Comparative Study
  • English Abstract

MeSH terms

  • Data Interpretation, Statistical
  • Databases, Protein
  • Hydrogen Bonding
  • Peptides / chemistry
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Thermodynamics

Substances

  • Peptides
  • Proteins