Electrostatic complementarity between proteins and ligands. 1. Charge disposition, dielectric and interface effects.
J Comput Aided Mol Des
; 8(5): 513-25, 1994 Oct.
Article
em En
| MEDLINE
| ID: mdl-7876898
ABSTRACT
Electrostatic interactions have always been considered an important factor governing ligand-receptor interactions. Previous work in this field has established the existence of electrostatic complementarity between the ligand and its receptor site. However, this property has not been treated rigorously, and the description remains largely qualitative. In this work, 34 data sets of high quality were chosen from the Brookhaven Protein Databank. The electrostatic complementary has been calculated between the surface potentials; complementarity is absent between adjacent or neighbouring atoms of the ligand and the receptor. There is little difference between complementarities on the total ligand surface and the interfacial region. Altering the homogeneous dielectric to distance-dependent dielectrics reduces the complementarity slightly, but does not affect the pattern of complementarity.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Ligantes
Tipo de estudo:
Prognostic_studies
/
Qualitative_research
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article