Ab initio fragment molecular orbital (FMO) method applied to analysis of the ligand-protein interaction in a pheromone-binding protein

Comput Biol Chem. 2005 Dec;29(6):434-9. doi: 10.1016/j.compbiolchem.2005.09.005. Epub 2005 Nov 10.

Abstract

Full quantum computation of the electronic state of proteins has recently become possible by the advent of the ab initio fragment molecular orbital (FMO) method. We applied this method to the analysis of the interaction between the Bombyx mori pheromone-binding protein and its ligand, bombykol. The protein-ligand interaction of this molecular complex was minutely analyzed by the FMO method, and the analysis revealed several important interactions between the ligand and amino acid residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bombyx
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Insect Proteins / chemistry
  • Insect Proteins / metabolism*
  • Ligands
  • Models, Molecular
  • Protein Binding

Substances

  • Carrier Proteins
  • Insect Proteins
  • Ligands
  • pheromone binding protein, insect