1H-NMR assignment and secondary structure of a herpes simplex virus glycoprotein D-1 antigenic domain

Eur J Biochem. 1986 Aug 1;158(3):527-36. doi: 10.1111/j.1432-1033.1986.tb09786.x.


The peptide alpha Ahx-Met-Ala-Asp-Pro-Asn-Arg-Phe-Arg-Gly-Lys-Asp-Leu-Pro-Val-Leu- Asp-Gln-Leu-Thr-Asp-Pro-Pro-alpha Ahx (epsilon Ahx = 6-aminohexanoyl), the antigenic sequence 11-32 from Herpes simplex virus glycoprotein D-1, has been synthesised. Its 1H-NMR spectrum has been assigned by a combination of two-dimensional techniques in H2O and 2H2O. Its secondary structure has been defined by nuclear Overhauser effects and amide proton exchange rates, and also to some extent chemical shifts, coupling constants and amide proton temperature coefficients. These latter parameters are shown to be less reliable as guides to secondary structure. The peptide has a helical (type I/III) turn at residues Pro-14-Asn-15 and helical structure at residues Lys-20-Val-24, in rapid equilibrium with random-coil structure. A beta-turn at residues Arg-18-Gly-19 may be present as a minor component. These locations of secondary structure correspond with previously determined regions of antigenic activity.

MeSH terms

  • Amides
  • Amino Acid Sequence
  • Epitopes / analysis*
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy
  • Protein Conformation
  • Spectrum Analysis
  • Temperature
  • Viral Envelope Proteins / immunology*


  • Amides
  • Epitopes
  • Viral Envelope Proteins
  • glycoprotein D, Human herpesvirus 1