Open AccessElectrostatic potential molecular surfaces.
Author(s) -
Paul K. Weiner,
Robert Langridge,
Jeffrey M. Blaney,
Ronald P. Schaefer,
Peter A. Kollman
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.12.3754
Subject(s) - netropsin , complementarity (molecular biology) , macromolecule , electrostatics , dna , chemistry , computer graphics , trypsin , molecular graphics , ligand (biochemistry) , biophysics , crystallography , biology , biochemistry , computer science , computer graphics (images) , genetics , enzyme , receptor , minor groove
Color-coded computer graphics representations of the electrostatic potentials of trypsin, trypsin-inhibitor, prealbumin and its thyroxine complex, fragments of double-helical DNA, and a netropsin--DNA complex illustrate the electrostatic and topographic complementarity in macromolecule-ligand interactions. This approach is powerful in revealing intermolecular specificity and shows promise of having predictive value in drug design.