Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation

Proteins. 1991;9(2):81-9. doi: 10.1002/prot.340090202.

Abstract

In our previous paper we reported the conformation of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 1H NMR experiment and distance geometry calculation. No hydrogen bonds were taken into consideration explicitly in the calculation. However, mostly alpha-helical conformations were obtained as results of the calculation even with no explicitly assumed hydrogen bonds. In the present paper we refined the distance geometry calculation by incorporating hydrogen bonds suggested by the previous calculation. As a result, we obtained the conformation of melittin, which was consistent with both NMR data and the additional hydrogen bonding data. The alpha-helical rod in the refined conformation also has a kink at Thr-11 and Gly-12, but its bent angle is now a bit narrowly distributed in 135 degrees +/- 15 degrees. In the present study another distortion at Trp-19 and IIe-20 becomes conspicuous. The average root-mean-square displacement of atoms is now much smaller and is 1.5 A for all backbone atoms. In the present paper side chain conformations are also analyzed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Deuterium / metabolism
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Melitten / chemistry*
  • Melitten / metabolism
  • Micelles*
  • Molecular Structure
  • Phosphorylcholine / analogs & derivatives*
  • Phosphorylcholine / chemistry
  • Phosphorylcholine / metabolism
  • Protein Conformation

Substances

  • Micelles
  • Phosphorylcholine
  • Melitten
  • dodecylphosphocholine
  • Deuterium